The domain within your query sequence starts at position 24 and ends at position 169; the E-value for the RHO domain shown below is 8.2e-75.

All catalytic sites are present in this domain. Check the literature (PubMed 11995995 ) for details.

CVVVGDGAVGKTCLLMSYANDAFPEEYVPTVFDHYAVTVTVGGKQHLLGLYDTAGQEDYN
QLRPLSYPNTDVFLICFSVVNPASYHNVQEEWVPELKDCMPHVPYVLIGTQIDLRDDPKT
LARLLYMKEKPLTYEHGVKLAKAVEN

RHO

Rho (Ras homology) subfamily of Ras-like small GTPases

• SMART accession number: SM00174
• Description: Members of this subfamily of Ras-like small GTPases include Cdc42 and Rac, as well as Rho isoforms.

There are 13543 RHO domains in 13489 proteins in SMART's nrdb database.

Cellular role (predicted cellular role)

Binding / catalysis: GTP-hydrolysis

Literature (relevant references for this domain)

Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

• Hall A
• Rho GTPases and the actin cytoskeleton.
• Science. 1998; 279: 509-14

The actin cytoskeleton mediates a variety of essential biological functions in all eukaryotic cells. In addition to providing a structural framework around which cell shape and polarity are defined, its dynamic properties provide the driving force for cells to move and to divide. Understanding the biochemical mechanisms that control the organization of actin is thus a major goal of contemporary cell biology, with implications for health and disease. Members of the Rho family of small guanosine triphosphatases have emerged as key regulators of the actin cytoskeleton, and furthermore, through their interaction with multiple target proteins, they ensure coordinated control of other cellular activities such as gene transcription and adhesion.

• Ren XD, Schwartz MA
• Regulation of inositol lipid kinases by Rho and Rac.
• Curr Opin Genet Dev. 1998; 8: 63-7

Rho and Rac small GTPases associate with type-I phosphatidylinositol 4-phosphate 5-kinase to regulate the production of phosphatidylinositol 4,5-bisphosphate. This lipid appears to mediate some of the effects of Rho and Rac on the actin cytoskeleton. The genes for several type-I phosphatidylinositol 4-phosphate 5-kinases have been cloned recently but it is not known which one interacts with Rho and/or Rac. Rho family GTPases also interact with phosphatidylinositol 3-kinase, though this kinase can be either upstream or downstream of the GTPases depending upon the system.

• Tanaka K, Takai Y
• Control of reorganization of the actin cytoskeleton by Rho family small GTP-binding proteins in yeast.
• Curr Opin Cell Biol. 1998; 10: 112-6

Accumulating evidence indicates that Rho family small GTP-binding proteins regulate reorganization of the actin cytoskeleton. There are members of the Rho family in the budding yeast Saccharomyces cerevisiae, in which powerful molecular genetical approaches are applicable. Recent identification of regulators and targets of the Rho family members has enhanced our understanding of the regulation and modes of action of Rho family members in reorganization of the actin cytoskeleton.

• Feltham JL et al.
• Definition of the switch surface in the solution structure of Cdc42Hs.
• Biochemistry. 1997; 36: 8755-66

Proteins of the rho subfamily of ras GTPases have been shown to be crucial components of pathways leading to cell growth and the establishment of cell polarity and mobility. Presented here is the solution structure of one such protein, Cdc42Hs, which provides insight into the structural basis for specificity of interactions between this protein and its effector and regulatory proteins. Standard heteronuclear NMR methods were used to assign the protein, and approximately 2100 distance and dihedral angle constraints were used to calculate a set of 20 structures using a combination of distance geometry and simulated annealing refinement. These structures show overall similarity to those of other GTP-binding proteins, with some exceptions. The regions corresponding to switch I and switch II in H-ras are disordered, and no evidence was found for an alpha-helix in switch II. The 13-residue insertion, which is only present in rho-subtype proteins and has been shown to be an important mediator of binding of regulatory and target proteins, forms a compact structure containing a short helix lying adjacent to the beta4-alpha3 loop. The insert forms one edge of a "switch surface" and, unexpectedly, does not change conformation upon activation of the protein by the exchange of GTP analogs for GDP. These studies indicate the insert region forms a stable invariant "footrest" for docking of regulatory and effector proteins.

• Hirshberg M, Stockley RW, Dodson G, Webb MR
• The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue.
• Nat Struct Biol. 1997; 4: 147-52

The crystal structure of human rac1, a member of the rho family of small G-proteins, complexed with the non-hydrolysable GTP analogue, guanosine-5'-(beta gamma-imino)triphosphate (GMPPNP), has been determined by X-ray analysis at a resolution of 1.38 A. Comparison with the structure of H-ras indicates that rac1 has an extra alpha-helical domain that is characteristic of the rho G proteins, and may be involved in the signalling pathway of this family.

• Koelle MR
• A new family of G-protein regulators - the RGS proteins.
• Curr Opin Cell Biol. 1997; 9: 143-7

Genetic experiments have recently been used to identify a family of 'regulator of G-protein signaling' (RGS) proteins, which downregulate signaling by heterotrimeric G proteins. The first biochemical studies of RGS proteins have shown that they accelerate the GTPase activities of G-protein alpha subunits, thus driving G proteins into their inactive GDP-bound forms. The physiological significance of the large number of different RGS proteins remains to be explored.

• Li R, Zhang B, Zheng Y
• Structural determinants required for the interaction between Rho GTPase and the GTPase-activating domain of p190.
• J Biol Chem. 1997; 272: 32830-5

The Rho family small GTP-binding proteins are subjected to regulation by Rho GTPase-activating proteins (GAPs) in the course of transmitting diverse intracellular signals. To understand the mechanism of GAP-catalyzed GTP hydrolysis of Rho GTPases, we have studied the interaction between RhoA and p190, the RasGAP binding phosphoprotein which has been implicated as a Rho-specific GAP, by delineating the structural determinants of RhoA and p190 GAP domain (p190GD) that are involved in their functional coupling. Besides the conserved residues Tyr34, Thr37, and Phe39 in the switch I region of RhoA which are required for p190GD interaction, chimeras made between RhoA and Cdc42, a close relative of RhoA with which p190GD interacts 50-fold less efficiently, revealed that residues outside the switch I and neighboring regions of RhoA, residues 85-122 in particular, contain the major p190GD-specifying determinant(s). Mutation of the unique Asp90 of RhoA in this region mostly abolished p190GD stimulation, whereas the corresponding reverse mutation of Cdc42 (S88D) was able to respond to p190GD-catalysis similarly as RhoA. Further kinetic analysis of these mutants provided evidence that Asp90 of RhoA contributes primarily to the specific binding interaction with p190GD. On the other hand, two charged residues of p190GD, Arg1283 and Lys1321, which are located in the putative G-protein binding helix pocket of GAP domain, were found to be involved in different aspects of interaction with RhoA. The R1283L mutant of p190GD lost GAP activity but retained the ability to bind to RhoA, while K1321A failed to stimulate and to bind to RhoA. These results indicate that residue Asp90 constitutes the second GAP-interactive site in RhoA which is mostly responsible for conferring p190GD-specificity, and suggest that the role of p190GD in the GTPase reaction of RhoA is in part to supply active site residue Arg1283 for efficient catalysis.

• Rittinger K, Walker PA, Eccleston JF, Smerdon SJ, Gamblin SJ
• Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue.
• Nature. 1997; 389: 758-62

Small G proteins of the Rho family, which includes Rho, Rac and Cdc42Hs, regulate phosphorylation pathways that control a range of biological functions including cytoskeleton formation and cell proliferation. They operate as molecular switches, cycling between the biologically active GTP-bound form and the inactive GDP-bound state. Their rate of hydrolysis of GTP to GDP by virtue of their intrinsic GTPase activity is slow, but can be accelerated by up to 10(5)-fold through interaction with rhoGAP, a GTPase-activating protein that stimulates Rho-family proteins. As such, rhoGAP plays a crucial role in regulating Rho-mediated signalling pathways. Here we report the crystal structure of RhoA and rhoGAP complexed with the transition-state analogue GDP.AlF4- at 1.65 A resolution. There is a rotation of 20 degrees between the Rho and rhoGAP proteins in this complex when compared with the ground-state complex Cdc42Hs.GMPPNP/rhoGAP, in which Cdc42Hs is bound to the non-hydrolysable GTP analogue GMPPNP. Consequently, in the transition state complex but not in the ground state, the rhoGAP domain contributes a residue, Arg85(GAP) directly into the active site of the G protein. We propose that this residue acts to stabilize the transition state of the GTPase reaction. RhoGAP also appears to function by stabilizing several regions of RhoA that are important in signalling the hydrolysis of GTP.

• Rittinger K et al.
• Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP.
• Nature. 1997; 388: 693-7

Small G proteins transduce signals from plasma-membrane receptors to control a wide range of cellular functions. These proteins are clustered into distinct families but all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of G proteins, which includes Cdc42Hs, activate effectors involved in the regulation of cytoskeleton formation, cell proliferation and the JNK signalling pathway. G proteins generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GTPase-activating proteins (GAPs) that enhance the rate of GTP hydrolysis by up to 10(5) times. We report here the crystal structure of Cdc42Hs, with the non-hydrolysable GTP analogue GMPPNP, in complex with the GAP domain of p50rhoGAP at 2.7A resolution. In the complex Cdc42Hs interacts, mainly through its switch I and II regions, with a shallow pocket on rhoGAP which is lined with conserved residues. Arg 85 of rhoGAP interacts with the P-loop of Cdc42Hs, but from biochemical data and by analogy with the G-protein subunit G(i alpha1), we propose that it adopts a different conformation during the catalytic cycle which enables it to stabilize the transition state of the GTP-hydrolysis reaction.

• Scheffzek K et al.
• The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants.
• Science. 1997; 277: 333-8

The three-dimensional structure of the complex between human H-Ras bound to guanosine diphosphate and the guanosine triphosphatase (GTPase)-activating domain of the human GTPase-activating protein p120GAP (GAP-334) in the presence of aluminum fluoride was solved at a resolution of 2.5 angstroms. The structure shows the partly hydrophilic and partly hydrophobic nature of the communication between the two molecules, which explains the sensitivity of the interaction toward both salts and lipids. An arginine side chain (arginine-789) of GAP-334 is supplied into the active site of Ras to neutralize developing charges in the transition state. The switch II region of Ras is stabilized by GAP-334, thus allowing glutamine-61 of Ras, mutation of which activates the oncogenic potential, to participate in catalysis. The structural arrangement in the active site is consistent with a mostly associative mechanism of phosphoryl transfer and provides an explanation for the activation of Ras by glycine-12 and glutamine-61 mutations. Glycine-12 in the transition state mimic is within van der Waals distance of both arginine-789 of GAP-334 and glutamine-61 of Ras, and even its mutation to alanine would disturb the arrangements of residues in the transition state.

• Sprang SR
• G protein mechanisms: insights from structural analysis.
• Annu Rev Biochem. 1997; 66: 639-78

This review is concerned with the structures and mechanisms of a superfamily of regulatory GTP hydrolases (G proteins). G proteins include Ras and its close homologs, translation elongation factors, and heterotrimeric G proteins. These proteins share a common structural core, exemplified by that of p21ras (Ras), and significant sequence identity, suggesting a common evolutionary origin. Three-dimensional structures of members of the G protein superfamily are considered in light of other biochemical findings about the function of these proteins. Relationships among G protein structures are discussed, and factors contributing to their low intrinsic rate of GTP hydrolysis are considered. Comparison of GTP- and GDP-bound conformations of G proteins reveals how specific contacts between the gamma-phosphate of GTP and the switch II region stabilize potential effector-binding sites and how GTP hydrolysis results in collapse (or reordering) of these surfaces. A GTPase-activating protein probably binds to and stabilizes the conformation of its cognate G protein that recognizes the transition state for hydrolysis, and may insert a catalytic residue into the G protein active site. Inhibitors of nucleotide release, such as the beta gamma subunit of a heterotrimeric G protein, bind selectively to and stabilize the GDP-bound state. Release factors, such as the translation elongation factor, Ts, also recognize the switch regions and destabilize the Mg(2+)-binding site, thereby promoting GDP release. G protein-coupled receptors are expected to operate by a somewhat different mechanism, given that the GDP-bound form of many G protein alpha subunits does not contain bound Mg2+.

• Sprang SR
• G proteins, effectors and GAPs: structure and mechanism.
• Curr Opin Struct Biol. 1997; 7: 849-56

G proteins from a diverse family of regulatory GTPases which, in the GTP-bound state, bind to and activate downstream effectors. Structures of Ras homologs bound to effector domains have revealed mechanisms by which G proteins couple GTP binding to effector activation and achieve specificity. Complexes between structurally unrelated GTPase-activating proteins with complementary G proteins suggest common mechanisms by which GTP hydrolysis is stimulated via direct interactions with conformationally labile switch regions of the G protein.

• Tesmer JJ, Berman DM, Gilman AG, Sprang SR
• Structure of RGS4 bound to AlF4--activated G(i alpha1): stabilization of the transition state for GTP hydrolysis.
• Cell. 1997; 89: 251-61

RGS proteins are GTPase activators for heterotrimeric G proteins. We report here the 2.8 A resolution crystal structure of the RGS protein RGS4 complexed with G(i alpha1)-Mg2+-GDP-AlF4 . Only the core domain of RGS4 is visible in the crystal. The core domain binds to the three switch regions of G(i alpha1), but does not contribute catalytic residues that directly interact with either GDP or AlF4-. Therefore, RGS4 appears to catalyze rapid hydrolysis of GTP primarily by stabilizing the switch regions of G(i alpha1), although the conserved Asn-128 from RGS4 could also play a catalytic role by interacting with the hydrolytic water molecule or the side chain of Gln-204. The binding site for RGS4 on G(i alpha1) is also consistent with the activity of RGS proteins as antagonists of G(alpha) effectors.

• Narumiya S
• The small GTPase Rho: cellular functions and signal transduction.
• J Biochem (Tokyo). 1996; 120: 215-28

Rho, a Ras homologue of small GTPase, is present from yeast to mammals. It shuttles between the active GTP-bound form and the inactive GDP-bound form and works as a switch in stimulus-evoked cell adhesion and motility, enhancement of contractile responses, and cytokinesis. In these actions, Rho directs the reorganization of the actin cytoskeleton at a specific time and at a specific site in the cell. It also activates serum response factor possibly via a kinase cascade and mediates a growth signal to nuclei. Two signalling processes are known to lead to Rho activation: one is activation of certain types of G-protein-coupled receptors such as lysophosphatidic acid receptor, and the other is activation of other small GTPases including Ras, CDC42, and Rac. Molecules catalyzing the GDP-GTP exchange of Rho, Rho guanine nucleotide exchange factors (Rho GEF), and those catalyzing the acceleration of GTP hydrolysis, Rho GTPase activating proteins (Rho GAP), were identified as Dbl- and Bcr-containing molecules, respectively. In addition, a molecule inhibiting guanine nucleotide exchange of Rho, Rho guanine nucleotide dissociation inhibitor (Rho-GDI), was isolated and characterized. More recently, putative Rho targets possibly mediating various Rho actions have been identified by their selective interaction with GTP-bound Rho. They include lipid kinases such as phosphatidyl-inositol-5-kinase and protein serine/threonine kinases such as PKN and p160ROCK. A model of the molecular mechanism of action of Rho constructed on the basis of these findings is presented. There are, however, still many unclarified links between cell stimulation, Rho activation and final Rho actions.

• Scheffzek K, Lautwein A, Kabsch W, Ahmadian MR, Wittinghofer A
• Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras.
• Nature. 1996; 384: 591-6

Ras-related GTP-binding proteins function as molecular switches which cycle between GTP-bound 'on'- and GDP-bound 'off'-states. GTP hydrolysis is the common timing mechanism that mediates the return from the 'on' to the 'off'-state. It is usually slow but can be accelerated by orders of magnitude upon interaction with GTPase-activating proteins (GAPs). In the case of Ras, a major regulator of cellular growth, point mutations are found in approximately 30% of human tumours which render the protein unable to hydrolyse GTP, even in the presence of Ras-GAPs. The first structure determination of a GTPase-activating protein reveals the catalytically active fragment of the Ras-specific p120GAP (ref. 2), GAP-334, as an elongated, exclusively helical protein which appears to represent a novel protein fold. The molecule consists of two domains, one of which contains all the residues conserved among different GAPs for Ras. From the location of conserved residues around a shallow groove in the central domain we can identify the site of interaction with Ras x GTP. This leads to a model for the interaction between Ras and GAP that satisfies numerous biochemical and genetic data on this important regulatory process.

• Watanabe G et al.
• Protein kinase N (PKN) and PKN-related protein rhophilin as targets of small GTPase Rho.
• Science. 1996; 271: 645-8

The Rho guanosine 5'-triphosphatase (GTPase) cycles between the active guanosine triphosphate (GTP)-bound form and the inactive guanosine diphosphate-bound form and regulates cell adhesion and cytokinesis, but how it exerts these actions is unknown. The yeast two-hybrid system was used to clone a complementary DNA for a protein (designated Rhophilin) that specifically bound to GTP-Rho. The Rho-binding domain of this protein has 40 percent identity with a putative regulatory domain of a protein kinase, PKN. PKN itself bound to GTP-Rho and was activated by this binding both in vitro and in vivo. This study indicates that a serine-threonine protein kinase is a Rho effector and presents an amino acid sequence motif for binding to GTP-Rho that may be shared by a family of Rho target proteins.

• Watson N, Linder ME, Druey KM, Kehrl JH, Blumer KJ
• RGS family members: GTPase-activating proteins for heterotrimeric G-protein alpha-subunits.
• Nature. 1996; 383: 172-5

Signaling pathways using heterotrimeric guanine-nucleotide-binding-proteins (G proteins) trigger physiological responses elicited by hormones, neurotransmitters and sensory stimuli. GTP binding activates G proteins by dissociating G alpha from G beta gamma subunits, and GTP hydrolysis by G alpha subunits deactivates G proteins by allowing heterotrimers to reform. However, deactivation of G-protein signalling pathways in vivo can occur 10- to 100-fold faster than the rate of GTP hydrolysis of G alpha subunits in vitro, suggesting that GTPase-activating proteins (GAPs) deactivate G alpha subunits. Here we report that RGS (for regulator of G-protein signalling) proteins are GAPs for G alpha subunits. RGS1, RGS4 and GAIP (for G alpha-interacting protein) bind specifically and tightly to G alphai and G alpha0 in cell membranes treated with GDP and AlF4(-), and are GAPs for G alphai, G alpha0 and transducin alpha-subunits, but not for G alphas. Thus, these RGS proteins are likely to regulate a subset of the G-protein signalling pathways in mammalian cells. Our results provide insight into the mechanisms that govern the duration and specificity of physiological responses elicited by G-protein-mediated signalling pathways.

• Zigmond SH
• Signal transduction and actin filament organization.
• Curr Opin Cell Biol. 1996; 8: 66-73

Small GTP-binding proteins of the Rho family appear to integrate extracellular signals from diverse receptor types and initiate rearrangements of F-actin. Active members of the Rho family, Rho and Rac, are now joined by Cdc42 which induces filopodia. Downstream of the Rho family proteins, actin polymerization may be induced by an increase in the availability of actin filament barbed ends. Actin organization may be affected by exposure of actin-binding sites on proteins such as vinculin and ezrin.

• Scheffzek K, Klebe C, Fritz-Wolf K, Kabsch W, Wittinghofer A
• Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form.
• Nature. 1995; 374: 378-81

The Ran proteins constitute a distinct branch of the superfamily of Ras-related GTP-binding proteins which function as molecular switches cycling between GTP-bound 'on' and GDP-bound 'off' states. Ran is located predominantly in the nucleus of eukaryotic cells and is involved in the nuclear import of proteins as well as in control of DNA synthesis and of cell-cycle progression. We report here the crystal structure at 2.3 A resolution of human Ran (Mr 24K) complexed with GDP and Mg2+. This structure reveals a similarity with the Ras core (G-domain) but with significant variations in regions involved in GDP and Mg2+ coordination (switch I and switch II regions in Ras), suggesting that there could be major conformational changes upon GTP binding. In addition to the G-domain, an extended chain and an alpha-helix were identified at the carboxy terminus. The amino-terminal (amino-acid residues MAAQGEP) stretch and the acidic tail (DEDDDL) appear to be flexible in the crystal structure.

Disease (disease genes where sequence variants are found in this domain)

SwissProt sequences and OMIM curated human diseases associated with missense mutations within the RHO domain.

Protein	Disease
Ras-related protein Rab-27A (P51159) (SMART)	OMIM:603868: Griscelli syndrome OMIM:214450:
GTPase HRas (P01112) (SMART)	OMIM:190020: Bladder cancer OMIM:109800:
GTPase NRas (P01111) (SMART)	OMIM:164790: Colorectal cancer
GTPase KRas (P01116) (SMART)	OMIM:190070: Colorectal adenoma ; Colorectal cancer
Ras-related protein R-Ras2 (P62070) (SMART)	OMIM:600098: ONCOGENE TC21
UNKNOWN (SMART)	OMIM:190070: Colorectal adenoma ; Colorectal cancer

Metabolism (metabolic pathways involving proteins which contain this domain)

% proteins involved	KEGG pathway ID	Description
9.21	map04360	Axon guidance
7.77	map04670	Leukocyte transendothelial migration
7.34	map04520	Adherens junction
7.34	map04510	Focal adhesion
7.34	map04810	Regulation of actin cytoskeleton
5.76	map04370	VEGF signaling pathway
5.76	map04010	MAPK signaling pathway
5.76	map05212	Pancreatic cancer
4.46	map05210	Colorectal cancer
4.46	map04530	Tight junction
4.46	map04310	Wnt signaling pathway
4.46	map04660	T cell receptor signaling pathway
4.17	map05120	Epithelial cell signaling in Helicobacter pylori infection
4.17	map05211	Renal cell carcinoma
2.88	map04664	Fc epsilon RI signaling pathway
2.88	map04662	B cell receptor signaling pathway
2.88	map04912	GnRH signaling pathway
2.88	map04650	Natural killer cell mediated cytotoxicity
1.58	map04350	TGF-beta signaling pathway
1.29	map05030	Amyotrophic lateral sclerosis (ALS)
1.29	map04620	Toll-like receptor signaling pathway
1.01	map04120	Ubiquitin mediated proteolysis
0.86	map04910	Insulin signaling pathway

This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with RHO domain which could be assigned to a KEGG orthologous group, and not all proteins containing RHO domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.

Structure (3D structures containing this domain)

3D Structures of RHO domains in PDB

PDB code	Title
1a2b	HUMAN RHOA COMPLEXED WITH GTP ANALOGUE
1a4r	G12V MUTANT OF HUMAN PLACENTAL CDC42 GTPASE IN THE GDP FORM
1aje	CDC42 FROM HUMAN, NMR, 20 STRUCTURES
1am4	COMPLEX BETWEEN CDC42HS.GMPPNP AND P50 RHOGAP (H. SAPIENS)
1an0	CDC42HS-GDP COMPLEX
1cc0	CRYSTAL STRUCTURE OF THE RHOA.GDP-RHOGDI COMPLEX
1cee	SOLUTION STRUCTURE OF CDC42 IN COMPLEX WITH THE GTPASE BINDING DOMAIN OF WASP
1cf4	CDC42/ACK GTPASE-BINDING DOMAIN COMPLEX
1cxz	CRYSTAL STRUCTURE OF HUMAN RHOA COMPLEXED WITH THE EFFECTOR DOMAIN OF THE PROTEIN KINASE PKN/PRK1
1doa	Structure of the rho family gtp-binding protein cdc42 in complex with the multifunctional regulator rhogdi
1dpf	CRYSTAL STRUCTURE OF A MG-FREE FORM OF RHOA COMPLEXED WITH GDP
1ds6	CRYSTAL STRUCTURE OF A RAC-RHOGDI COMPLEX
1e0a	Cdc42 complexed with the GTPase binding domain of p21 activated kinase
1e96	Structure of the Rac/p67phox complex
1ees	SOLUTION STRUCTURE OF CDC42HS COMPLEXED WITH A PEPTIDE DERIVED FROM P-21 ACTIVATED KINASE, NMR, 20 STRUCTURES
1foe	CRYSTAL STRUCTURE OF RAC1 IN COMPLEX WITH THE GUANINE NUCLEOTIDE EXCHANGE REGION OF TIAM1
1ftn	CRYSTAL STRUCTURE OF THE HUMAN RHOA/GDP COMPLEX
1g4u	CRYSTAL STRUCTURE OF THE SALMONELLA TYROSINE PHOSPHATASE AND GTPASE ACTIVATING PROTEIN SPTP BOUND TO RAC1
1grn	CRYSTAL STRUCTURE OF THE CDC42/CDC42GAP/ALF3 COMPLEX.
1gwn	The crystal structure of the core domain of RhoE/Rnd3 - a constitutively activated small G protein
1gzs	CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE GEF DOMAIN OF THE SALMONELLA TYPHIMURIUM SOPE TOXIN AND HUMAN Cdc42
1he1	Crystal structure of the complex between the GAP domain of the Pseudomonas aeruginosa ExoS toxin and human Rac
1hh4	Rac1-RhoGDI complex involved in NADPH oxidase activation
1i4d	CRYSTAL STRUCTURE ANALYSIS OF RAC1-GDP COMPLEXED WITH ARFAPTIN (P21)
1i4l	CRYSTAL STRUCTURE ANALYSIS OF RAC1-GDP IN COMPLEX WITH ARFAPTIN (P41)
1i4t	CRYSTAL STRUCTURE ANALYSIS OF RAC1-GMPPNP IN COMPLEX WITH ARFAPTIN
1ki1	Guanine Nucleotide Exchange Region of Intersectin in Complex with Cdc42
1kmq	Crystal Structure of a Constitutively Activated RhoA Mutant (Q63L)
1kz7	Crystal Structure of the DH/PH Fragment of Murine Dbs in Complex with the Placental Isoform of Human Cdc42
1kzg	DbsCdc42(Y889F)
1lb1	Crystal Structure of the Dbl and Pleckstrin homology domains of Dbs in complex with RhoA
1m7b	Crystal structure of Rnd3/RhoE: functional implications
1mh1	SMALL G-PROTEIN
1nf3	Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity protein, Par6
1ow3	Crystal Structure of RhoA.GDP.MgF3-in Complex with RhoGAP
1ryf	Alternative Splicing of Rac1 Generates Rac1b, a Self-activating GTPase
1ryh	Alternative Splicing of Rac1 Generates Rac1b, a Self-activating GTPase
1s1c	Crystal structure of the complex between the human RhoA and Rho-binding domain of human ROCKI
1tx4	RHO/RHOGAP/GDP(DOT)ALF4 COMPLEX
1x86	Crystal Structure of the DH/PH domains of Leukemia-associated RhoGEF in complex with RhoA
1xcg	Crystal Structure of Human RhoA in complex with DH/PH fragment of PDZRHOGEF
1z2c	Crystal structure of mDIA1 GBD-FH3 in complex with RhoC-GMPPNP
2ase	NMR structure of the F28L mutant of Cdc42Hs
2atx	Crystal Structure of the TC10 GppNHp complex
2c2h	CRYSTAL STRUCTURE OF THE HUMAN RAC3 IN COMPLEX WITH GDP
2cls	The crystal structure of the human RND1 GTPase in the active GTP bound state
2dfk	Crystal structure of the CDC42-Collybistin II complex
2fju	Activated Rac1 bound to its effector phospholipase C beta 2
2fv8	The crystal structure of RhoB in the GDP-bound state
2g0n	The Crystal Structure of the Human RAC3 in complex with GDP and Chloride
2gcn	Crystal structure of the human RhoC-GDP complex
2gco	Crystal structure of the human RhoC-GppNHp complex
2gcp	Crystal structure of the human RhoC-GSP complex
2h7v	Co-crystal structure of YpkA-Rac1
2ic5	Crystal structure of human RAC3 grown in the presence of Gpp(NH)p.
2j0v	The crystal structure of Arabidopsis thaliana RAC7-ROP9: the first RAS superfamily GTPase from the plant kingdom
2j1l	Crystal Structure of Human Rho-related GTP-binding protein RhoD
2kb0	Cdc42(T35A)
2ngr	TRANSITION STATE COMPLEX FOR GTP HYDROLYSIS BY CDC42: COMPARISONS OF THE HIGH RESOLUTION STRUCTURES FOR CDC42 BOUND TO THE ACTIVE AND CATALYTICALLY COMPROMISED FORMS OF THE CDC42-GAP.
2nty	Rop4-GDP-PRONE8
2nz8	N-terminal DHPH cassette of Trio in complex with nucleotide-free Rac1
2odb	The crystal structure of human cdc42 in complex with the CRIB domain of human p21-activated kinase 6 (PAK6)
2ov2	The crystal structure of the human RAC3 in complex with the CRIB domain of human p21-activated kinase 4 (PAK4)
2p2l	Rac1-GDP-Zinc Complex
2q3h	The crystal structure of RhouA in the GDP-bound state.
2qme	Crystal structure of human RAC3 in complex with CRIB domain of human p21-activated kinase 1 (PAK1)
2qrz	Cdc42 bound to GMP-PCP: Induced Fit by Effector is Required
2rex	Crystal structure of the effector domain of PLXNB1 bound with Rnd1 GTPase
2rgn	Crystal Structure of p63RhoGEF complex with Galpha-q and RhoA
2rmk	Rac1/PRK1 Complex
2v55	Mechanism of multi-site phosphorylation from a ROCK-I:RhoE complex structure
2vrw	Critical structural role for the PH and C1 domains of the Vav1 exchange factor
2w2t	Rac2 (G12V) in complex with GDP
2w2v	Rac2 (G12V) in complex with GTPgS
2w2x	Complex of Rac2 and PLCg2 spPH Domain
2wbl	Three-dimensional structure of a binary ROP-PRONE complex
2wkp	Structure of a photoactivatable Rac1 containing Lov2 Wildtype
2wkq	Structure of a photoactivatable Rac1 containing the Lov2 C450A Mutant
2wkr	Structure of a photoactivatable Rac1 containing the Lov2 C450M Mutant
2wm9	Structure of the complex between DOCK9 and Cdc42.
2wmn	Structure of the complex between DOCK9 and Cdc42-GDP.
2wmo	Structure of the complex between DOCK9 and Cdc42.
2yin	STRUCTURE OF THE COMPLEX BETWEEN Dock2 AND Rac1.
3a58	Crystal structure of Sec3p - Rho1p complex from Saccharomyces cerevisiae
3b13	Crystal structure of the DHR-2 domain of DOCK2 in complex with Rac1 (T17N mutant)
3bji	Structural Basis of Promiscuous Guanine Nucleotide Exchange by the T-Cell Essential Vav1
3bwd	Crystal structure of the plant Rho protein ROP5
3eg5	Crystal structure of MDIA1-TSH GBD-FH3 in complex with CDC42-GMPPNP
3gcg	crystal structure of MAP and CDC42 complex
3kz1	Crystal Structure of the Complex of PDZ-RhoGEF DH/PH domains with GTP-gamma-S Activated RhoA
3lw8	Shigella IpgB2 in complex with human RhoA, GDP and Mg2+ (complex A)
3lwn	Shigella IpgB2 in complex with human RhoA, GDP and Mg2+ (complex B)
3lxr	Shigella IpgB2 in complex with human RhoA and GDP (complex C)
3msx	Crystal structure of RhoA.GDP.MgF3 in complex with GAP domain of ArhGAP20
3q3j	Crystal structure of plexin A2 RBD in complex with Rnd1
3qbv	Structure of designed orthogonal interaction between CDC42 and nucleotide exchange domains of intersectin
3ref	Crystal structure of EhRho1 bound to GDP and Magnesium
3reg	Crystal structure of EhRho1 bound to a GTP analog and Magnesium
3ryt	The Plexin A1 intracellular region in complex with Rac1
3sbd	Crystal structure of RAC1 P29S mutant
3sbe	Crystal structure of RAC1 P29S mutant
3su8	Crystal structure of a truncated intracellular domain of Plexin-B1 in complex with Rac1
3sua	Crystal structure of the intracellular domain of Plexin-B1 in complex with Rac1
3t06	Crystal Structure of the DH/PH fragment of PDZRHOGEF with N-terminal regulatory elements in complex with Human RhoA
3th5	Crystal structure of wild-type RAC1
3tvd	Crystal Structure of Mouse RhoA-GTP complex
3vhl	Crystal structure of the DHR-2 domain of DOCK8 in complex with Cdc42 (T17N mutant)
4d0n	AKAP13 (AKAP-Lbc) RhoGEF domain in complex with RhoA
4did	Crystal structure of Salmonella effector N-terminal domain SopB in complex with Cdc42
4dvg	Crystal structure of E. histolytica Formin1 bound to EhRho1-GTPgammaS
4f38	Crystal structure of geranylgeranylated RhoA in complex with RhoGDI in its active GPPNHP-bound form
4gzl	Crystal structure of RAC1 Q61L mutant
4gzm	Crystal structure of RAC1 F28L mutant
4itr	Crystal Structure of IbpAFic2-H3717A in complex with adenylylated Cdc42
4js0	Complex of Cdc42 with the CRIB-PR domain of IRSp53
4mit	4MIT
4u5x	4U5X
4xh9	4XH9
4xoi	4XOI
4xsg	4XSG
4xsh	4XSH
4yc7	4YC7
4ydh	4YDH
4yon	4YON
5a0f	5A0F
5bwm	5BWM
5c2j	5C2J
5c2k	5C2K
5c4m	5C4M
5cjp	5CJP
5fi0	5FI0
5fi1	5FI1
5fr1	5FR1
5fr2	5FR2
5hpy	5HPY
5irc	5IRC
5jcp	5JCP