The domain within your query sequence starts at position 344 and ends at position 376; the E-value for the WW domain shown below is 3.29e-4.

VPGSPWCVVWTGDDRVFFFNPTMQLSVWEKPVD

WW

Domain with 2 conserved Trp (W) residues

• SMART accession number: SM00456
• Description: Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
• Interpro abstract (IPR001202):

  Synonym(s): Rsp5 or WWP domain

  The WW domain is a short conserved region in a number of unrelated proteins, which folds as a stable, triple stranded beta-sheet. This short domain of approximately 40 amino acids, may be repeated up to four times in some proteins [ (PUBMED:7846762) (PUBMED:7802651) (PUBMED:7828727) (PUBMED:7641887) ]. The name WW or WWP derives from the presence of two signature tryptophan residues that are spaced 20-23 amino acids apart and are present in most WW domains known to date, as well as that of a conserved Pro. The WW domain binds to proteins with particular proline-motifs, [AP]-P-P-[AP]-Y, and/or phosphoserine- phosphothreonine-containing motifs [ (PUBMED:7644498) (PUBMED:11911877) ]. It is frequently associated with other domains typical for proteins in signal transduction processes.

  A large variety of proteins containing the WW domain are known. These include; dystrophin, a multidomain cytoskeletal protein; utrophin, a dystrophin-like protein of unknown function; vertebrate YAP protein, substrate of an unknown serine kinase; Mus musculus (Mouse) NEDD-4, involved in the embryonic development and differentiation of the central nervous system; Saccharomyces cerevisiae (Baker's yeast) RSP5, similar to NEDD-4 in its molecular organisation; Rattus norvegicus (Rat) FE65, a transcription-factor activator expressed preferentially in liver; Nicotiana tabacum (Common tobacco) DB10 protein, amongst others.

• GO function: protein binding (GO:0005515)

There are 67566 WW domains in 38399 proteins in SMART's nrdb database.

Cellular role (predicted cellular role)

Cellular role: interaction, signalling
Binding / catalysis: protein-binding, polyproline-binding

Literature (relevant references for this domain)

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

• Bedford MT, Reed R, Leder P
• WW domain-mediated interactions reveal a spliceosome-associated protein that binds a third class of proline-rich motif: the proline glycine and methionine-rich motif.
• Proc Natl Acad Sci U S A. 1998; 95: 10602-7

Pre-mRNA splicing requires the bridging of the 5' and 3' ends of the intron. In yeast, this bridging involves interactions between the WW domains in the splicing factor PRP40 and a proline-rich domain in the branchpoint binding protein, BBP. Using a proline-rich domain derived from formin (a product of the murine limb deformity locus), we have identified a family of murine formin binding proteins (FBP's), each of which contains one or more of a special class of tyrosine-rich WW domains. Two of these WW domains, in the proteins FBP11 and FBP21, are strikingly similar to those found in the yeast splicing factor PRP40. We show that FBP21 is present in highly purified spliceosomal complex A, is associated with U2 snRNPs, and colocalizes with splicing factors in nuclear speckle domains. Moreover, FBP21 interacts directly with the U1 snRNP protein U1C, the core snRNP proteins SmB and SmB', and the branchpoint binding protein SF1/mBBP. Thus, FBP21 may play a role in cross-intron bridging of U1 and U2 snRNPs in the mammalian A complex.

• Neele DM, Kaptein A, Huisman H, deWit EC, Princen HM
• No effect of fibrates on synthesis of apolipoprotein(a) in primary cultures of cynomolgus monkey and human hepatocytes: apolipoprotein A-I synthesis increased.
• Biochem Biophys Res Commun. 1998; 244: 374-8

Fibrates have been shown to decrease plasma levels of triglyceride-rich lipoproteins and LDL and to increase HDL. Data on the effect of fibrates on lipoprotein(a) levels in man are not consistent. Because lp(a) levels in vivo are mainly regulated at synthesis level, we studied the effect of fibrates on the synthesis of apolipoprotein(a) (apo(a)) in primary cultures of cynomolgus monkey and human hepatocytes. Furthermore, we assessed the effect of fibrates on apolipoprotein A-I (apo A-I) synthesis and investigated whether different fibrates have different effects on the apo(a) and apo A-I synthesis. The addition of gemfibrozil to cultures of monkey and human hepatocytes had no effect on apo(a) synthesis, but resulted in a dose- and time-dependent increase of apo A-I synthesis and mRNA. In simian hepatocytes maximal stimulation was 2.5-fold after incubation for 72 h with 1.0 mM gemfibrozil, whereas apo A-I synthesis was induced 1.8- and 2.0-fold by using 0.1 mM and 0.3 mM, respectively. Similar results were obtained by using human hepatocytes; apo(a) synthesis remained unchanged, while apo A-I secretion was 2.0-fold increased at 1 mM gemfibrozil. Other fibrates like bezafibrate, clofibrate and clofibric acid did not change apo(a) synthesis either. In contrast, they enhanced the synthesis of apo A-I (1.5-, 1.8- and 1.8-fold, respectively), although less potently than gemfibrozil. We conclude that fibrates have no effect on apolipoprotein(a) synthesis in monkey and human hepatocytes and that these drugs induce apo A-I synthesis.

• Rotin D
• WW (WWP) domains: from structure to function.
• Curr Top Microbiol Immunol. 1998; 228: 115-33

• DiFiore PP, Pelicci PG, Sorkin A
• EH: a novel protein-protein interaction domain potentially involved in intracellular sorting.
• Trends Biochem Sci. 1997; 22: 411-3

• Ermekova KS et al.
• The WW domain of neural protein FE65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled.
• J Biol Chem. 1997; 272: 32869-77

The neural protein FE65 contains two types of protein-protein interaction modules: one WW binding domain and two phosphotyrosine binding domains. The carboxyl-terminal phosphotyrosine binding domain of FE65 interacts in vivo with the beta-amyloid precursor protein, which is implicated in Alzheimer disease. To understand the function of this adapter protein, we identified binding partners for the FE65 WW domain. Proline-rich sequences sharing a proline-proline-leucine-proline core motif were recovered by screening expression libraries for ligands of the FE65 WW domain. Five proteins of molecular masses 60, 75, 80, 140, and 200 kDa could be purified from mouse brain lysates by affinity to the FE65 WW domain. We identified two of these five proteins as the 80- and 140-kDa isoforms encoded by Mena, the mammalian homolog of the Drosophila Enabled gene. Using the SPOTs technique of peptide synthesis, we identified the sequences in Mena that interact with the FE65 WW domain and found that they contain the signature proline-proline-leucine-proline motif. Finally, we demonstrated that Mena binds to FE65 in vivo by coimmunoprecipitation assay from COS cell extracts. The specificity of the Mena-FE65 WW domain association was confirmed by competition assays. Further characterization of the FE65-Mena complex may identify a physiological role for these proteins in beta-amyloid precursor protein biogenesis and may help in understanding the mechanism of molecular changes that underlie Alzheimer disease.

• Gavva NR, Gavva R, Ermekova K, Sudol M, Shen CJ
• Interaction of WW domains with hematopoietic transcription factor p45/NF-E2 and RNA polymerase II.
• J Biol Chem. 1997; 272: 24105-8

NF-E2 is an erythroid-specific transcription factor required for expression of several erythroid-specific genes. By Far-Western blotting and yeast two-hybrid assay, we demonstrate that p45, the large subunit of NF-E2, is capable of binding to a specific set of WW domain-containing proteins, including the ubiquitin ligase hRPF1. This binding is mediated through the interaction between the WW domains and a PY motif located within the amino-terminal region of p45. Interestingly, the carboxyl-terminal domain of mammalian RNA polymerase II binds a similar set of WW domains to which p45 interacts with. We discuss the data in terms of possible new pathways through which the processes of transcriptional regulation by NF-E2 could be regulated in erythroid and megakaryote cells.

• Macias MJ et al.
• Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide.
• Nature. 1996; 382: 646-9

The WW domain is a new protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro. It is present in a number of signalling and regulatory proteins, often in several copies. Here we investigate the solution structure of the WW domain of human YAP65 (for Yes kinase-associated protein) in complex with proline-rich peptides containing the core motif PPxY. The structure of the domain with the bound peptide GTPPPPYTVG is a slightly curved, three-stranded, antiparallel beta-sheet. Two prolines pack against the first tryptophan, forming a hydrophobic buckle on the convex side of the sheet. The concave side has three exposed hydrophobic residues (tyrosine, tryptophan and leucine) which form the binding site for the ligand. A non-conserved isoleucine in the amino-terminal flanking region covers a hydrophobic patch and stabilizes the WW domain of human YAP65 in vitro. The structure of the WW domain differs from that of the SH3 domain and reveals a new design for a protein module that uses stacked aromatic surface residues to arrange a binding site for proline-rich peptides.

• Ponting CP, Blake DJ, Davies KE, Kendrick-Jones J, Winder SJ
• ZZ and TAZ: new putative zinc fingers in dystrophin and other proteins.
• Trends Biochem Sci. 1996; 21: 11-13

• Hofmann K, Bucher P
• The rsp5-domain is shared by proteins of diverse functions.
• FEBS Lett. 1995; 358: 153-7

A novel, unusually small, and highly conserved domain of modular intracellular proteins is described. The domain was first recognized as three repeats in the yeast rsp5 gene product and named thereafter. The rsp5 protein is thought to interact with nuclear proteins but also contains a C2 domain typical for cytoplasmic proteins. Further analyses revealed several additional occurrences of this domain in diverse protein classes, including cytoplasmic signal transduction proteins, gene products interacting with the transcription machinery, structural proteins like dystrophin, and a putative RNA helicase.

• Sudol M et al.
• Characterization of the mammalian YAP (Yes-associated protein) gene and its role in defining a novel protein module, the WW domain.
• J Biol Chem. 1995; 270: 14733-41

We report cDNA cloning and characterization of the human and mouse orthologs of the chicken YAP (Yes-associated protein) gene which encodes a novel protein that binds to the SH3 (Src homology 3) domain of the Yes proto-oncogene product. Sequence comparison between mouse, human, and chicken YAP proteins showed an inserted sequence in the mouse YAP that represented an imperfect repeat of an upstream sequence. Further analysis of this sequence revealed a putative protein module that is found in various structural, regulatory, and signaling molecules in yeast, nematode, and mammals including human dystrophin. Because one of the prominent features of this sequence motif is two tryptophans (W), we named it the WW domain (Bork, P., and Sudol, M. (1994) Trends Biochem. Sci. 19, 531-533). Since its delineation, more proteins have been shown to contain this domain, and we report here on the widespread distribution of the WW module and present a discussion of its possible function. We have also shown that the human YAP gene is well conserved among higher eukaryotes, but it may not be conserved in yeast. Its expression at the RNA level in adult human tissues is nearly ubiquitous, being relatively high in placenta, prostate, ovary, and testis, but is not detectable in peripheral blood leukocytes. Using fluorescence in situ hybridization on human metaphase chromosomes and by analyzing rodent-human hybrids by Southern blot hybridization and polymerase chain reaction amplification, we mapped the human YAP gene to chromosome band 11q13, a region to which the multiple endocrine neoplasia type 1 gene has been mapped.

• Andre B, Springael JY
• WWP, a new amino acid motif present in single or multiple copies in various proteins including dystrophin and the SH3-binding Yes-associated protein YAP65.
• Biochem Biophys Res Commun. 1994; 205: 1201-5

A new repeating amino acid motif, which we called WWP, was found in several proteins of yeast, nematod or vertebrate origin. Among these are dystrophin, the product of the Duchenne muscular dystrophy locus, a protein (YAP65) which associates in vitro with the Src homology domain 3 (SH3) of the Yes proto-oncogene product, and a human putative GTPase-activating protein. As is the case for proteins which contain the SH2, SH3 and PH domains, at least some of the WWP-containing proteins appear to be signaling or cytoskeletal proteins, associated with plasma or organellar membranes, and specific protein-protein contacts are likely to be crucial to their function.

• Bork P, Sudol M
• The WW domain: a signalling site in dystrophin?
• Trends Biochem Sci. 1994; 19: 531-3

• Kobe B, Deisenhofer J
• The leucine-rich repeat: a versatile binding motif.
• Trends Biochem Sci. 1994; 19: 415-21

Leucine-rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. All proteins containing these repeats are thought to be involved in protein-protein interactions. The crystal structure of ribonuclease inhibitor protein has revealed that leucine-rich repeats correspond to beta-alpha structural units. These units are arranged so that they form a parallel beta-sheet with one surface exposed to solvent, so that the protein acquires an unusual, nonglobular shape. These two features may be responsible for the protein-binding functions of proteins containing leucine-rich repeats.

• Maclennan AJ, Shaw G
• A yeast SH2 domain.
• Trends Biochem Sci. 1993; 18: 464-5

Metabolism (metabolic pathways involving proteins which contain this domain)

% proteins involved	KEGG pathway ID	Description
23.53	map04120	Ubiquitin mediated proteolysis
21.57	map05050	Dentatorubropallidoluysian atrophy (DRPLA)
15.69	map04530	Tight junction
10.78	map04350	TGF-beta signaling pathway
5.88	map05010	Alzheimer's disease
3.92	map04810	Regulation of actin cytoskeleton
1.96	map00260	Glycine, serine and threonine metabolism
1.96	map00625	Tetrachloroethene degradation
1.96	map00650	Butanoate metabolism
1.96	map00591	Linoleic acid metabolism
1.96	map00052	Galactose metabolism
1.96	map00120	Bile acid biosynthesis
1.96	map00380	Tryptophan metabolism
1.96	map00363	Bisphenol A degradation
1.96	map00051	Fructose and mannose metabolism
0.98	map00230	Purine metabolism

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 WW domain which could be assigned to a KEGG orthologous group, and not all proteins containing WW 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 WW domains in PDB

PDB code	Title
1e0l	FBP28WW domain from Mus musculus
1e0m	PROTOTYPE WW domain
1eg3	STRUCTURE OF A DYSTROPHIN WW DOMAIN FRAGMENT IN COMPLEX WITH A BETA-DYSTROGLYCAN PEPTIDE
1eg4	STRUCTURE OF A DYSTROPHIN WW DOMAIN FRAGMENT IN COMPLEX WITH A BETA-DYSTROGLYCAN PEPTIDE
1f8a	STRUCTURAL BASIS FOR THE PHOSPHOSERINE-PROLINE RECOGNITION BY GROUP IV WW DOMAINS
1i5h	SOLUTION STRUCTURE OF THE RNEDD4 WWIII DOMAIN-RENAC BP2 PEPTIDE COMPLEX
1i6c	SOLUTION STRUCTURE OF PIN1 WW DOMAIN
1i8g	SOLUTION STRUCTURE OF PIN1 WW DOMAIN COMPLEXED WITH CDC25 PHOSPHOTHREONINE PEPTIDE
1i8h	SOLUTION STRUCTURE OF PIN1 WW DOMAIN COMPLEXED WITH HUMAN TAU PHOSPHOTHREONINE PEPTIDE
1jmq	YAP65 (L30K mutant) WW domain in Complex with GTPPPPYTVG peptide
1k5r	YAP65 WW domain S24-Amino-Ethylsulfanyl-Acetic Acid mutant
1k9q	YAP65 WW domain complexed to N-(n-octyl)-GPPPY-NH2
1k9r	YAP65 WW domain complexed to Acetyl-PLPPY
1nmv	Solution structure of human Pin1
1o6w	Solution Structure of the Prp40 WW Domain Pair of the Yeast Splicing Factor Prp40
1pin	PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FROM HOMO SAPIENS
1tk7	NMR structure of WW domains (WW3-4) from Suppressor of Deltex
1wmv	Solution structure of the second WW domain of WWOX
1wr3	Solution structure of the first WW domain of Nedd4-2
1wr4	Solution structure of the second WW domain of Nedd4-2
1wr7	Solution structure of the third WW domain of Nedd4-2
1yiu	Itch E3 ubiquitin ligase WW3 domain
1ymz	CC45, An Artificial WW Domain Designed Using Statistical Coupling Analysis
1yw5	Peptidyl-prolyl isomerase ESS1 from Candida albicans
1ywi	Structure of the FBP11WW1 domain complexed to the peptide APPTPPPLPP
1ywj	Structure of the FBP11WW1 domain
1zcn	human Pin1 Ng mutant
1zr7	Solution structure of the first WW domain of FBP11
2djy	Solution structure of Smurf2 WW3 domain-Smad7 PY peptide complex
2dk1	Solution structure of WW domain in WW domain binding protein 4 (WBP-4)
2dk7	Solution structure of WW domain in transcription elongation regulator 1
2dmv	Solution structure of the second ww domain of Itchy homolog E3 ubiquitin protein ligase (Itch)
2dwv	Solution structure of the second WW domain from mouse salvador homolog 1 protein (mWW45)
2dyf	Solution structure of the first WW domain of FBP11 / HYPA (FBP11 WW1) complexed with a PL (PPLP) motif peptide ligand
2e45	Solution structure of Fe65 WW domain
2ez5	Solution Structure of the dNedd4 WW3* Domain- Comm LPSY Peptide Complex
2f21	human Pin1 Fip mutant
2ho2	Structure of human FE65-WW domain in complex with hMena peptide.
2idh	Crystal Structure of human FE65 WW domain
2itk	human Pin1 bound to D-PEPTIDE
2jmf	Solution structure of the Su(dx) WW4- Notch PY peptide complex
2jo9	Mouse Itch 3rd WW domain complex with the Epstein-Barr virus latent membrane protein 2A derived peptide EEPPPPYED
2joc	Mouse Itch 3rd domain phosphorylated in T30
2jup	FBP28WW2 domain in complex with the PPLIPPPP peptide
2jv4	Structure Characterisation of PINA WW Domain and Comparison with other Group IV WW Domains, PIN1 and ESS1
2jx8	Solution structure of hPCIF1 WW domain
2jxw	Solution Structure of the Tandem WW Domains of FBP21
2kbu	NMR solution structure of Pin1 WW domain mutant with beta turn mimic at position 12
2kcf	The NMR solution structure of the isolated Apo Pin1 WW domain
2kpz	Human NEDD4 3RD WW Domain Complex with The Human T-cell Leukemia virus 1 GAG-Pro poliprotein Derived Peptide SDPQIPPPYVEP
2kq0	Human NEDD4 3rd WW Domain Complex with Ebola Zaire Virus Matrix Protein VP40 Derived Peptide ILPTAPPEYMEA
2kxq	Solution Structure of Smurf2 WW2 and WW3 bound to Smad7 PY motif containing peptide
2kyk	The sandwich region between two LMP2A PY motif regulates the interaction between AIP4WW2domain and PY motif
2l4j	Yap ww2
2l5f	Solution structure of the tandem WW domains from HYPA/FBP11
2laj	Third WW domain of human Nedd4L in complex with doubly phosphorylated human smad3 derived peptide
2law	Structure of the second WW domain from human YAP in complex with a human Smad1 derived peptide
2lax	Structure of first WW domain of human YAP in complex with a human Smad1 doubly-phosphorilated derived peptide.
2lay	Structure of the first WW domain of human YAP in complex with a phosphorylated human Smad1 derived peptide
2laz	Structure of the first WW domain of human Smurf1 in complex with a mono-phosphorylated human Smad1 derived peptide
2lb0	Structure of the first WW domain of human Smurf1 in complex with a di-phosphorylated human Smad1 derived peptide
2lb1	Structure of the second domain of human Smurf1 in complex with a human Smad1 derived peptide
2lb2	Structure of the second domain of human Nedd4L in complex with a phosphorylated pTPY motif derived from human Smad3
2lb3	Structure of the WW domain of PIN1 in complex with a human phosphorylated Smad3 derived peptide
2ltv	YAP WW2 in complex with a Smad7 derived peptide
2ltw	YAP WW1 in complex with a Smad7 derived peptide
2ltx	Smurf1 WW2 domain in complex with a Smad7 derived peptide
2lty	NEDD4L WW2 domain in complex with a Smad7 derived peptide
2ltz	Smurf2 WW3 domain in complex with a Smad7 derived peptide
2m3o	Structure and dynamics of a human Nedd4 WW domain-ENaC complex
2m8i	Structure of Pin1 WW domain
2m8j	Structure of Pin1 WW domain phospho-mimic S16E
2m9e	NMR solution structure of Pin1 WW domain mutant 5-1
2m9f	NMR solution structure of Pin1 WW domain mutant 5-1g
2m9i	NMR solution structure of Pin1 WW domain variant 6-1
2m9j	NMR solution structure of Pin1 WW domain mutant 6-1g
2mdc	2MDC
2mdi	2MDI
2mdj	2MDJ
2mpt	2MPT
2mw9	2MW9
2mwa	2MWA
2mwb	2MWB
2mwd	2MWD
2mwe	2MWE
2mwf	2MWF
2n1o	2N1O
2n4r	2N4R
2n4s	2N4S
2n4t	2N4T
2n4u	2N4U
2n4v	2N4V
2n4w	2N4W
2n8s	2N8S
2n8t	2N8T
2n8u	2N8U
2nc3	2NC3
2nc4	2NC4
2nc5	2NC5
2nc6	2NC6
2nnt	General structural motifs of amyloid protofilaments
2oei	Crystal structure of human FE65-WW domain in complex with human Mena peptide
2op7	WW4
2q5a	human Pin1 bound to L-PEPTIDE
2rly	FBP28WW2 domain in complex with PTPPPLPP peptide
2rm0	FBP28WW2 domain in complex with a PPPLIPPPP peptide
2xp3	DISCOVERY OF CELL-ACTIVE PHENYL-IMIDAZOLE PIN1 INHIBITORS BY STRUCTURE-GUIDED FRAGMENT EVOLUTION
2xp4	DISCOVERY OF CELL-ACTIVE PHENYL-IMIDAZOLE PIN1 INHIBITORS BY STRUCTURE-GUIDED FRAGMENT EVOLUTION
2xp5	DISCOVERY OF CELL-ACTIVE PHENYL-IMIDAZOLE PIN1 INHIBITORS BY STRUCTURE-GUIDED FRAGMENT EVOLUTION
2xp6	DISCOVERY OF CELL-ACTIVE PHENYL-IMIDAZOLE PIN1 INHIBITORS BY STRUCTURE-GUIDED FRAGMENT EVOLUTION
2xp7	DISCOVERY OF CELL-ACTIVE PHENYL-IMIDAZOLE PIN1 INHIBITORS BY STRUCTURE-GUIDED FRAGMENT EVOLUTION
2xp8	DISCOVERY OF CELL-ACTIVE PHENYL-IMIDAZOLE PIN1 INHIBITORS BY STRUCTURE-GUIDED FRAGMENT EVOLUTION
2xp9	DISCOVERY OF CELL-ACTIVE PHENYL-IMIDAZOLE PIN1 INHIBITORS BY STRUCTURE-GUIDED FRAGMENT EVOLUTION
2xpa	DISCOVERY OF CELL-ACTIVE PHENYL-IMIDAZOLE PIN1 INHIBITORS BY STRUCTURE-GUIDED FRAGMENT EVOLUTION
2xpb	DISCOVERY OF CELL-ACTIVE PHENYL-IMIDAZOLE PIN1 INHIBITORS BY STRUCTURE-GUIDED FRAGMENT EVOLUTION
2ysb	Solution structure of the first WW domain from the mouse salvador homolog 1 protein (SAV1)
2ysc	Solution structure of the WW domain from the human amyloid beta A4 precursor protein-binding family B member 3, APBB3
2ysd	Solution structure of the first WW domain from the human membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1. MAGI-1
2yse	Solution structure of the second WW domain from the human membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1. MAGI-1
2ysf	Solution structure of the fourth WW domain from the human E3 ubiquitin-protein ligase Itchy homolog, ITCH
2ysg	Solution structure of the WW domain from the human syntaxin-binding protein 4
2ysh	Solution structure of the WW domain from the human growth-arrest-specific protein 7, GAS-7
2ysi	Solution structure of the first WW domain from the mouse transcription elongation regulator 1, transcription factor CA150
2zaj	Solution structure of the short-isoform of the second WW domain from the human membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 (MAGI-1)
2zqs	Crystal structure of a mutant PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE
2zqt	Crystal structure of a mutant PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE
2zqu	Crystal structure of a mutant PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE
2zqv	Crystal structure of a mutant PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE
2zr4	Crystal structure of a mutant PIN1 peptidyl-prolyl cis-trans isomerase
2zr5	Crystal structure of a mutant PIN1 peptidyl-prolyl cis-trans isomerase
2zr6	Crystal structure of a mutant PIN1 peptidyl-prolyl cis-trans isomerase
3kab	Structure-guided design of alpha-amino acid-derived Pin1 inhibitors
3kad	Structure-guided design of alpha-amino acid-derived Pin1 inhibitors
3kaf	Structure-guided design of alpha-amino acid-derived Pin1 inhibitors
3kag	Structure-guided design of alpha-amino acid-derived Pin1 inhibitors
3kah	Structure-guided design of alpha-amino acid-derived Pin1 inhibitors
3kai	Structure-guided design of alpha-amino acid-derived Pin1 inhibitors
3kce	Structure-guided design of alpha-amino acid-derived Pin1 inhibitors
3l4h	Helical box domain and second WW domain of the human E3 ubiquitin-protein ligase HECW1
3le4	Crystal structure of the DGCR8 dimerization domain
3ntp	Human Pin1 complexed with reduced amide inhibitor
3odk	Discovery of cell-active phenyl-imidazole Pin1 inhibitors by structure-guided fragment evolution
3olm	Structure and Function of a Ubiquitin Binding Site within the Catalytic Domain of a HECT Ubiquitin Ligase
3oob	Structural and functional insights of directly targeting Pin1 by Epigallocatechin-3-gallate
3tc5	Selective targeting of disease-relevant protein binding domains by O-phosphorylated natural product derivatives
3tcz	Human Pin1 bound to cis peptidomimetic inhibitor
3tdb	Human Pin1 bound to trans peptidomimetic inhibitor
3wh0	3WH0
4e5r	Crystal Structure of Frog DGCR8 Dimerization Domain
4gwt	Structure of racemic Pin1 WW domain cocrystallized with DL-malic acid
4gwv	Structure of racemic Pin1 WW domain cocrystallized with tri-ammonium citrate
4lcd	Structure of an Rsp5xUbxSna3 complex: Mechanism of ubiquitin ligation and lysine prioritization by a HECT E3
4n7f	Crystal structure of 3rd WW domain of human Nedd4-1
4n7h	Crystal Structure of the Complex of 3rd WW domain of Human Nedd4 and 1st PPXY Motif of ARRDC3
4qib	4QIB
4rex	4REX
4rof	4ROF
4u84	4U84
4u85	4U85
4u86	4U86
5aht	5AHT
5b3z	5B3Z
5cq2	5CQ2
5dws	5DWS
5dzd	5DZD

Links (links to other resources describing this domain)

• INTERPRO: IPR001202
• PFAM: WW_rsp5_WWP
• PROSITE: WW_DOMAIN_2