CAScCaspase, interleukin-1 beta converting enzyme (ICE) homologues |
![]() |
---|
SMART accession number: | SM00115 |
---|---|
Description: | Cysteine aspartases that mediate programmed cell death (apoptosis). Caspases are synthesised as zymogens and activated by proteolysis of the peptide backbone adjacent to an aspartate. The resulting two subunits associate to form an (alpha)2(beta)2-tetramer which is the active enzyme. Activation of caspases can be mediated by other caspase homologues. |
Interpro abstract (IPR015917): | This group of sequences represent the core of p45 (45 kDa) precursor of caspases, which can be processed to produce the active p20 (20 kDa) and p10 (10 kDa) subunits. Caspases (Cysteine-dependent ASPartyl-specific proteASE) are cysteine peptidases that belong to the MEROPS peptidase family C14 (caspase family, clan CD) based on the architecture of their catalytic dyad or triad [(PUBMED:11517925)]. Caspases are tightly regulated proteins that require zymogen activation to become active, and once active can be regulated by caspase inhibitors. Activated caspases act as cysteine proteases, using the sulphydryl group of a cysteine side chain for catalysing peptide bond cleavage at aspartyl residues in their substrates. The catalytic cysteine and histidine residues are on the p20 subunit after cleavage of the p45 precursor. Caspases are mainly involved in mediating cell death (apoptosis) [(PUBMED:10578171), (PUBMED:10872455), (PUBMED:15077141)]. They have two main roles within the apoptosis cascade: as initiators that trigger the cell death process, and as effectors of the process itself. Caspase-mediated apoptosis follows two main pathways, one extrinsic and the other intrinsic or mitochondrial-mediated. The extrinsic pathway involves the stimulation of various TNF (tumour necrosis factor) cell surface receptors on cells targeted to die by various TNF cytokines that are produced by cells such as cytotoxic T cells. The activated receptor transmits the signal to the cytoplasm by recruiting FADD, which forms a death-inducing signalling complex (DISC) with caspase-8. The subsequent activation of caspase-8 initiates the apoptosis cascade involving caspases 3, 4, 6, 7, 9 and 10. The intrinsic pathway arises from signals that originate within the cell as a consequence of cellular stress or DNA damage. The stimulation or inhibition of different Bcl-2 family receptors results in the leakage of cytochrome c from the mitochondria, and the formation of an apoptosome composed of cytochrome c, Apaf1 and caspase-9. The subsequent activation of caspase-9 initiates the apoptosis cascade involving caspases 3 and 7, among others. At the end of the cascade, caspases act on a variety of signal transduction proteins, cytoskeletal and nuclear proteins, chromatin-modifying proteins, DNA repair proteins and endonucleases that destroy the cell by disintegrating its contents, including its DNA. The different caspases have different domain architectures depending upon where they fit into the apoptosis cascades, however they all carry the catalytic p10 and p20 subunits. Caspases can have roles other than in apoptosis, such as caspase-1 (interleukin-1 beta convertase) (EC 3.4.22.36), which is involved in the inflammatory process. The activation of apoptosis can sometimes lead to caspase-1 activation, providing a link between apoptosis and inflammation, such as during the targeting of infected cells. Caspases may also be involved in cell differentiation [(PUBMED:15066636)]. |
GO process: | apoptotic process (GO:0006915) |
GO function: | cysteine-type peptidase activity (GO:0008234) |
Family alignment: |
There are 2045 CASc domains in 2020 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
-
Taxonomic distribution of proteins containing CASc domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with CASc domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing CASc domain in the selected taxonomic class.
- Literature (relevant references for this domain)
-
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Liang H, Fesik SW
- Three-dimensional structures of proteins involved in programmed cell death.
- J Mol Biol. 1997; 274: 291-302
- Display abstract
Programmed cell death (apoptosis) is a controlled process by which unwanted cells are selectively eliminated. Several families of proteins including the Bcl-2, tumor necrosis factor receptor 1, and caspase families play essential roles in the regulation, signaling, and execution of the genetic cell death program. The recently described three-dimensional structures of members of these families elucidate the structural basis of their functions and provide insights into the mechanisms by which these proteins regulate apoptosis.
- Miller DK, Myerson J, Becker JW
- The interleukin-1 beta converting enzyme family of cysteine proteases.
- J Cell Biochem. 1997; 64: 2-10
- Display abstract
Interleukin-1 beta converting enzyme (ICE) is the first enzyme of a new family of cysteine endoproteinases to be isolated and characterized. An overview of the structure and activity of ICE is outlined together with highlights of salient features common to members of each of the family members.
- Villa P, Kaufmann SH, Earnshaw WC
- Caspases and caspase inhibitors.
- Trends Biochem Sci. 1997; 22: 388-93
- Display abstract
Five years ago, little was known about mechanisms of apoptotic execution. Now, one class of cell-death gene, the cysteine and aspartases (caspases) has come under intensive study. This review discusses the two classes of caspases, the reasons why humans may have so many caspase genes, the growing list of caspase substrates, and viral and pharmacological caspase inhibitors.
- Komiyama T et al.
- Inhibition of interleukin-1 beta converting enzyme by the cowpox virus serpin CrmA. An example of cross-class inhibition.
- J Biol Chem. 1994; 269: 19331-7
- Display abstract
We reported previously that human interleukin-1 beta converting enzyme (ICE) is regulated by the CrmA serpin encoded by cowpox virus. We now report the mechanism and kinetics of this unusual inhibition of a cysteine proteinase by a member of the serpin superfamily previously thought to inhibit serine proteinase only. CrmA possesses several characteristics typical of a number of inhibitory serpins. It is conformationally unstable, unfolding around 3 M urea, and stable to denaturation in 8 M urea upon complex formation with ICE. CrmA rapidly inhibits ICE with an association rate constant (kon) of 1.7 x 10(7) M-1 s-1, forming a tight complex with an equilibrium constant for inhibition (Ki) of less than 4 x 10(-12) M. These data indicate that CrmA is a potent inhibitor of ICE, consistent with the dramatic effects of CrmA on modifying host responses to virus infection. The inhibition of ICE by CrmA is an example of a "cross-class" interaction, in which a serpin inhibits a non-serine proteinase. Since CrmA possesses characteristics shared by inhibitors of serine proteinases, we presume that ICE, though it is a cysteine proteinase, has a substrate binding geometry strikingly close to that of serine proteinases. We reason that it is the substrate binding geometry, not the catalytic mechanism of a proteinase, that dictates its reactivity with protein inhibitors.
- Walker NP et al.
- Crystal structure of the cysteine protease interleukin-1 beta-converting enzyme: a (p20/p10)2 homodimer.
- Cell. 1994; 78: 343-52
- Display abstract
Interleukin-1 beta-converting enzyme (ICE) proteolytically cleaves pro-IL-1 beta to its mature, active form. The crystal structure at 2.5 A resolution of a recombinant human ICE-tetrapeptide chloromethylketone complex reveals that the holoenzyme is a homodimer of catalytic domains, each of which contains a p20 and a p10 subunit. The spatial separation of the C-terminus of p20 and the N-terminus of p10 in each domain suggests two alternative pathways of assembly and activation in vivo. ICE is homologous to the C. elegans cell death gene product, CED-3, and these may represent a novel class of cytoplasmic cysteine proteases that are important in programmed cell death (apoptosis). Conservation among members of the ICE/CED-3 family of the amino acids that form the active site region of ICE supports the hypothesis that they share functional similarities.
- Wilson KP et al.
- Structure and mechanism of interleukin-1 beta converting enzyme.
- Nature. 1994; 370: 270-5
- Display abstract
Interleukin-1 beta converting enzyme (ICE) processes an inactive precursor to the proinflammatory cytokine, interleukin-1 beta, and may regulate programmed cell death in neuronal cells. The high-resolution structure of human ICE in complex with an inhibitor has been determined by X-ray diffraction. The structure confirms the relationship between human ICE and cell-death proteins in other organisms. The active site spans both the 10 and 20K subunits, which associate to form a tetramer, suggesting a mechanism for ICE autoactivation.
- Miura M, Zhu H, Rotello R, Hartwieg EA, Yuan J
- Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3.
- Cell. 1993; 75: 653-60
- Display abstract
The mammalian interleukin-1 beta-converting enzyme (ICE) has sequence similarity to the C. elegans cell death gene ced-3. We show here that overexpression of the murine ICE (mICE) gene or of the C. elegans ced-3 gene causes Rat-1 cells to undergo programmed cell death. Point mutations in a region homologous between mICE and CED-3 eliminate the ability of mICE and ced-3 to cause cell death. The cell death caused by mICE can be suppressed by overexpression of the crmA gene, a specific inhibitor of ICE, as well as by bcl-2, a mammalian oncogene that can act to prevent programmed cell death. Our results suggest that ICE may function during mammalian development to cause programmed cell death.
- Yuan J, Shaham S, Ledoux S, Ellis HM, Horvitz HR
- The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme.
- Cell. 1993; 75: 641-52
- Display abstract
We have cloned the C. elegans cell death gene ced-3. A ced-3 transcript is most abundant during embryogenesis, the stage during which most programmed cell deaths occur. The predicted CED-3 protein shows similarity to human and murine interleukin-1 beta-converting enzyme and to the product of the mouse nedd-2 gene, which is expressed in the embryonic brain. The sequences of 12 ced-3 mutations as well as the sequences of ced-3 genes from two related nematode species identify sites of potential functional importance. We propose that the CED-3 protein acts as a cysteine protease in the initiation of programmed cell death in C. elegans and that cysteine proteases also function in programmed cell death in mammals.
- Cerretti DP et al.
- Molecular cloning of the interleukin-1 beta converting enzyme.
- Science. 1992; 256: 97-100
- Display abstract
Interleukin-1 beta (IL-1 beta) mediates a wide range of immune and inflammatory responses. The active cytokine is generated by proteolytic cleavage of an inactive precursor. A complementary DNA encoding a protease that carries out this cleavage has been cloned. Recombinant expression in COS-7 cells enabled the cells to process precursor IL-1 beta to the mature form. Sequence analysis indicated that the enzyme itself may undergo proteolytic processing. The gene encoding the protease was mapped to chromosomal band 11q23, a site frequently involved in rearrangement in human cancers.
- Thornberry NA et al.
- A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes.
- Nature. 1992; 356: 768-74
- Display abstract
Interleukin-1 beta (IL-1 beta)-converting enzyme cleaves the IL-1 beta precursor to mature IL-1 beta, an important mediator of inflammation. The identification of the enzyme as a unique cysteine protease and the design of potent peptide aldehyde inhibitors are described. Purification and cloning of the complementary DNA indicates that IL-1 beta-converting enzyme is composed of two nonidentical subunits that are derived from a single proenzyme, possibly by autoproteolysis. Selective inhibition of the enzyme in human blood monocytes blocks production of mature IL-1 beta, indicating that it is a potential therapeutic target.
- Metabolism (metabolic pathways involving proteins which contain this domain)
-
% proteins involved KEGG pathway ID Description 22.05 map04210 Apoptosis 12.93 map05050 Dentatorubropallidoluysian atrophy (DRPLA) 12.55 map05040 Huntington's disease 9.51 map04115 p53 signaling pathway 7.22 map05010 Alzheimer's disease 6.08 map05210 Colorectal cancer 3.42 map05120 Epithelial cell signaling in Helicobacter pylori infection 3.42 map04620 Toll-like receptor signaling pathway 3.42 map04010 MAPK signaling pathway 3.42 map04650 Natural killer cell mediated cytotoxicity 2.66 map05222 Small cell lung cancer 2.66 map05213 Endometrial cancer 2.66 map04370 VEGF signaling pathway 2.66 map05212 Pancreatic cancer 2.66 map05215 Prostate cancer 2.66 map05223 Non-small cell lung cancer 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 CASc domain which could be assigned to a KEGG orthologous group, and not all proteins containing CASc 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 CASc domains in PDB
PDB code Main view Title 1bmq CRYSTAL STRUCTURE OF THE COMPLEX OF INTERLEUKIN-1BETA CONVERTING ENZYME (ICE) WITH A PEPTIDE BASED INHIBITOR, (3S )-N-METHANESULFONYL-3-({1-[N-(2-NAPHTOYL)-L-VALYL]-L-PROLYL }AMINO)-4-OXOBUTANAMIDE 1cp3 CRYSTAL STRUCTURE OF THE COMPLEX OF APOPAIN WITH THE TETRAPEPTIDE INHIBITOR ACE-DVAD-FMC 1f1j CRYSTAL STRUCTURE OF CASPASE-7 IN COMPLEX WITH ACETYL-ASP-GLU-VAL-ASP-CHO 1f9e CASPASE-8 SPECIFICITY PROBED AT SUBSITE S4: CRYSTAL STRUCTURE OF THE CASPASE-8-Z-DEVD-CHO 1gfw THE 2.8 ANGSTROM CRYSTAL STRUCTURE OF CASPASE-3 (APOPAIN OR CPP32)IN COMPLEX WITH AN ISATIN SULFONAMIDE INHIBITOR. 1gqf Crystal structure of human procaspase-7 1i3o CRYSTAL STRUCTURE OF THE COMPLEX OF XIAP-BIR2 AND CASPASE 3 1i4e CRYSTAL STRUCTURE OF THE CASPASE-8/P35 COMPLEX 1i4o CRYSTAL STRUCTURE OF THE XIAP/CASPASE-7 COMPLEX 1i51 CRYSTAL STRUCTURE OF CASPASE-7 COMPLEXED WITH XIAP 1ibc CRYSTAL STRUCTURE OF INHIBITED INTERLEUKIN-1BETA CONVERTING ENZYME 1ice STRUCTURE AND MECHANISM OF INTERLEUKIN-1BETA CONVERTING ENZYME 1jxq Structure of cleaved, CARD domain deleted Caspase-9 1k86 Crystal structure of caspase-7 1k88 Crystal structure of procaspase-7 1kmc Crystal Structure of the Caspase-7 / XIAP-BIR2 Complex 1m72 Crystal Structure of Caspase-1 from Spodoptera frugiperda 1nme Structure of Casp-3 with tethered salicylate 1nmq Extendend Tethering: In Situ Assembly of Inhibitors 1nms Caspase-3 tethered to irreversible inhibitor 1nw9 STRUCTURE OF CASPASE-9 IN AN INHIBITORY COMPLEX WITH XIAP-BIR3 1pau CRYSTAL STRUCTURE OF THE COMPLEX OF APOPAIN WITH THE TETRAPEPTIDE ALDEHYDE INHIBITOR AC-DEVD-CHO 1pyo Crystal Structure of Human Caspase-2 in Complex with Acetyl-Leu-Asp-Glu-Ser-Asp-cho 1qdu CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-8 WITH THE TRIPEPTIDE KETONE INHIBITOR ZEVD-DCBMK 1qtn CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-8 WITH THE TETRAPEPTIDE INHIBITOR ACE-IETD-ALDEHYDE 1qx3 Conformational restrictions in the active site of unliganded human caspase-3 1re1 CRYSTAL STRUCTURE OF CASPASE-3 WITH A NICOTINIC ACID ALDEHYDE INHIBITOR 1rhj CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-3 WITH A PRYAZINONE INHIBITOR 1rhk Crystal structure of the complex of caspase-3 with a phenyl-propyl-ketone inhibitor 1rhm CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-3 WITH A NICOTINIC ACID ALDEHYDE INHIBITOR 1rhq CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-3 WITH A BROMOMETHOXYPHENYL INHIBITOR 1rhr CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-3 WITH A CINNAMIC ACID METHYL ESTER INHIBITOR 1rhu CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-3 WITH A 5,6,7 TRICYCLIC PEPTIDOMIMETIC INHIBITOR 1rwk Crystal structure of human caspase-1 in complex with 3-(2-mercapto-acetylamino)-4-oxo-pentanoic acid 1rwm Crystal structure of human caspase-1 in complex with 4-oxo-3-[2-(5-{[4-(quinoxalin-2-ylamino)-benzoylamino]-methyl}-thiophen-2-yl)-acetylamino]-pentanoic acid 1rwn Crystal structure of human caspase-1 in complex with 3-{2-ethyl-6-[4-(quinoxalin-2-ylamino)-benzoylamino]-hexanoylamino}-4-oxo-butyric acid 1rwo Crystal structure of human caspase-1 in complex with 4-oxo-3-{6-[4-(quinoxalin-2-ylamino)-benzoylamino]-2-thiophen-2-yl-hexanoylamino}-pentanoic acid 1rwp Crystal structure of human caspase-1 in complex with 3-{6-[(8-hydroxy-quinoline-2-carbonyl)-amino]-2-thiophen-2-yl-hexanoylamino}-4-oxo-butyric acid 1rwv Crystal structure of human caspase-1 in complex with 5-[5-(1-carboxymethyl-2-oxo-propylcarbamoyl)-5-phenyl-pentylsulfamoyl]-2-hydroxy-benzoic acid 1rww Crystal structure of human caspase-1 in complex with 4-oxo-3-[(6-{[4-(quinoxalin-2-ylamino)-benzoylamino]-methyl}-pyridine-3-carbonyl)-amino]-butyric acid 1rwx Crystal structure of human caspase-1 in complex with 4-oxo-3-{6-[4-(quinoxalin-2-yloxy)-benzoylamino]-2-thiophen-2-yl-hexanoylamino}-butyric acid 1sc1 Crystal structure of an active-site ligand-free form of the human caspase-1 C285A mutant 1sc3 Crystal structure of the human caspase-1 C285A mutant in complex with malonate 1sc4 Crystal structure of the human caspase-1 C285A mutant after removal of malonate 1shj Caspase-7 in complex with DICA allosteric inhibitor 1shl CASPASE-7 IN COMPLEX WITH FICA ALLOSTERIC INHIBITOR 2ar9 Crystal structure of a dimeric caspase-9 2c1e Crystal structures of caspase-3 in complex with aza-peptide Michael acceptor inhibitors. 2c2k Crystal structures of caspase-3 in complex with aza-peptide Michael acceptor inhibitors. 2c2m Crystal structures of caspase-3 in complex with aza-peptide Michael acceptor inhibitors. 2c2o Crystal structures of caspase-3 in complex with aza-peptide Michael acceptor inhibitors. 2c2z Crystal structure of caspase-8 in complex with aza-peptide Michael acceptor inhibitor 2cdr Crystal structures of caspase-3 in complex with aza-peptide epoxide inhibitors. 2cjx Extended substrate recognition in caspase-3 revealed by high resolution X-ray structure analysis 2cjy Extended substrate recognition in caspase-3 revealed by high resolution X-ray structure analysis 2cnk Crystal structures of caspase-3 in complex with aza-peptide epoxide inhibitors. 2cnl Crystal structures of caspase-3 in complex with aza-peptide epoxide inhibitors. 2cnn Crystal structures of caspase-3 in complex with aza-peptide epoxide inhibitors. 2cno Crystal structures of caspase-3 in complex with aza-peptide epoxide inhibitors. 2dko Extended substrate recognition in caspase-3 revealed by high resolution X-ray structure analysis 2fp3 Crystal structure of the Drosophila initiator caspase Dronc 2fqq Crystal structure of human caspase-1 (Cys285->Ala, Cys362->Ala, Cys364->Ala, Cys397->Ala) in complex with 1-methyl-3-trifluoromethyl-1H-thieno[2,3-c]pyrazole-5-carboxylic acid (2-mercapto-ethyl)-amide 2fun alternative p35-caspase-8 complex 2h48 Crystal structure of human caspase-1 (Cys362->Ala, Cys364->Ala, Cys397->Ala) in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK) 2h4w Crystal structure of human caspase-1 (Glu390->Asp) in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK) 2h4y Crystal structure of human caspase-1 (Arg286->Lys) in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK) 2h51 Crystal structure of human caspase-1 (Glu390->Asp and Arg286->Lys) in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK) 2h54 Crystal structure of human caspase-1 (Thr388->Ala) in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK) 2h5i Crystal structure of caspase-3 with inhibitor Ac-DEVD-Cho 2h5j Crystal strusture of caspase-3 with inhibitor Ac-DMQD-Cho 2h65 Crystal strusture of caspase-3 with inhibitor Ac-VDVAD-Cho 2hbq Crystal structure of wildtype human caspase-1 in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK) 2hbr Crystal structure of human caspase-1 (Arg286->Ala) in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK) 2hby Crystal structure of human caspase-1 (Glu390->Ala) in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK) 2hbz Crystal structure of human caspase-1 (Arg286->Ala, Glu390->Ala) in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK) 2j30 The Role of Loop Bundle Hydrogen Bonds in the Maturation and Activity of (Pro)caspase-3 2j31 The Role of Loop Bundle Hydrogen Bonds in the Maturation and Activity of(Pro)caspase-3 2j32 The Role of Loop Bundle Hydrogen Bonds in the Maturation and Activity of(Pro)caspase-3 2j33 The Role of Loop Bundle Hydrogen Bonds in the Maturation and Activity of (Pro)caspase-3 2k7z Solution Structure of the Catalytic Domain of Procaspase-8 2nn3 structure of pro-sf-caspase-1 2p2c Inhibition of caspase-2 by a designed ankyrin repeat protein (DARPin) 2ql5 Crystal Structure of caspase-7 with inhibitor AC-DMQD-CHO 2ql7 Crystal Structure of Caspase-7 with inhibitor AC-IEPD-CHO 2ql9 Crystal Structure of Caspase-7 with inhibitor AC-DQMD-CHO 2qlb Crystal Structure of caspase-7 with inhibitor AC-ESMD-CHO 2qlf Crystal Structure of Caspase-7 with inhibitor AC-DNLD-CHO 2qlj Crystal Structure of Caspase-7 with Inhibitor AC-WEHD-CHO 2wdp Crystal Structure of Ligand Free Human Caspase-6 2xyg Caspase-3:CAS329306 2xyh Caspase-3:CAS60254719 2xyp Caspase-3:CAS26049945 2xzd Caspase-3 in Complex with an Inhibitory DARPin-3.4 2xzt Caspase-3 in Complex with DARPin-3.4_I78S 2y0b Caspase-3 in Complex with an Inhibitory DARPin-3.4_S76R 2y1l Caspase-8 in Complex with DARPin-8.4 3d6f Crystal structure of human caspase-1 with a naturally-occurring Arg240->Gln substitution in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK) 3d6h Crystal structure of human caspase-1 with a naturally-occurring Asn263->Ser substitution in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK) 3d6m Crystal structure of human caspase-1 with a naturally-occurring Lys319->Arg substitution in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK) 3deh Crystal Structures of Caspase-3 with Bound Isoquinoline-1,3,4-trione Derivative Inhibitors 3dei Crystal Structures of Caspase-3 with Bound Isoquinoline-1,3,4-trione Derivative Inhibitors 3dej Crystal Structures of Caspase-3 with Bound Isoquinoline-1,3,4-trione Derivative Inhibitors 3dek Crystal Structures of Caspase-3 with Bound Isoquinoline-1,3,4-trione Derivative Inhibitors 3e4c Procaspase-1 zymogen domain crystal strucutre 3edq Crystal structure of Caspase-3 with inhibitor AC-LDESD-CHO 3edr The crystal structure of caspase-7 in complex with Acetyl-LDESD-CHO 3gjq Caspase-3 Binds Diverse P4 Residues in Peptides 3gjr Caspase-3 Binds Diverse P4 Residues in Peptides 3gjs Caspase-3 Binds Diverse P4 Residues in Peptides 3gjt Caspase-3 Binds Diverse P4 Residues in Peptides 3h0e 3,4-Dihydropyrimido(1,2-a)indol-10(2H)-ones as Potent Non-Peptidic Inhibitors of Caspase-3 3h11 Zymogen caspase-8:c-FLIPL protease domain complex 3h13 c-FLIPL protease-like domain 3h1p Mature Caspase-7 I213A with DEVD-CHO inhibitor bound to active site 3ibc Crystal Structure of Caspase-7 incomplex with Acetyl-YVAD-CHO 3ibf Crystal structure of unliganded caspase-7 3itn Crystal structure of Pseudo-activated Procaspase-3 3j9k 3J9K 3k7e Crystal structure of human ligand-free mature caspase-6 3kjf Caspase 3 Bound to a covalent inhibitor 3kjn Caspase 8 bound to a covalent inhibitor 3kjq Caspase 8 with covalent inhibitor 3nkf Crystal structure of human ligand-free mature caspase-6 with intersubunit linker attached 3nr2 Crystal structure of Caspase-6 zymogen 3ns7 Succinic Acid Amides as P2-P3 Replacements for Inhibitors of Interleukin-1beta Converting Enzyme (ICE or Caspase 1) 3od5 Crystal structure of active caspase-6 bound with Ac-VEID-CHO 3p45 Crystal structure of apo-caspase-6 at physiological pH 3p4u Crystal structure of active caspase-6 in complex with Ac-VEID-CHO inhibitor 3pcx Caspase-3 E246A, K242A Double Mutant 3pd0 Caspase-3 E246A 3pd1 Caspase-3 K242A 3qnw Caspase-6 in complex with Z-VAD-FMK inhibitor 3r5j Crystal structure of active caspase-2 bound with Ac-ADVAD-CHO 3r5k A designed redox-controlled caspase-7 3r6g Crystal structure of active caspase-2 bound with Ac-VDVAD-CHO 3r6l Caspase-2 T380A bound with Ac-VDVAD-CHO 3r7b Caspase-2 bound to one copy of Ac-DVAD-CHO 3r7n Caspase-2 bound with two copies of Ac-DVAD-CHO 3r7s Crystal Structure of Apo Caspase2 3rjm CASPASE2 IN COMPLEX WITH CHDI LIGAND 33c 3s70 Crystal structure of active caspase-6 bound with Ac-VEID-CHO solved by As-SAD 3s8e Phosphorylation regulates assembly of the caspase-6 substrate-binding groove 3sip Crystal structure of drICE and dIAP1-BIR1 complex 3sir Crystal Structure of drICE 3uo8 Crystal structure of the MALT1 paracaspase (P1 form) 3uoa Crystal structure of the MALT1 paracaspase (P21 form) 3v3k Human caspase 9 in complex with bacterial effector protein 3v4o Human MALT1 (caspase domain) in complex with an irreversible peptidic inhibitor 3v55 Human MALT1 (334-719) in its ligand free form 3v6l Crystal Structure of caspase-6 inactivation mutation 3v6m Inhibition of caspase-6 activity by single mutation outside the active site 4dcj Crystal structure of caspase 3, L168D mutant 4dco Crystal Structure of caspase 3, L168Y mutant 4dcp Crystal Structure of caspase 3, L168F mutant 4eha Allosteric Modulation of Caspase-3 through Mutagenesis 4ehd Allosteric Modulation of Caspase-3 through Mutagenesis 4ehf Allosteric Modulation of Caspase-3 through Mutagenesis 4ehh Allosteric Modulation of Caspase-3 through Mutagenesis 4ehk Allosteric Modulation of Caspase-3 through Mutagenesis 4ehl Allosteric Modulation of Caspase-3 through Mutagenesis 4ehn Allosteric Modulation of Caspase-3 through Mutagenesis 4ejf Allosteric peptides that bind to a caspase zymogen and mediate caspase tetramerization 4fdl Crystal structure of Caspase-7 4fea Crystal structure of CASPASE-7 in Complex with allosteric inhibitor 4fxo Zinc-mediated allosteric inhibiton of caspase-6 4hq0 Crystal Structure of mutant form of Caspase-7 4hqr Crystal Structure of mutant form of Caspase-7 4hva Mechanistic and Structural Understanding of Uncompetitive Inhibitors of Caspase-6 4i1p 4I1P 4i1r Human MALT1 (caspase-IG3) in complex with thioridazine 4iyr Crystal structure of full-length caspase-6 zymogen 4jb8 Caspase-7 in Complex with DARPin C7_16 4jj7 Caspase-3 specific unnatural amino acid-based peptides 4jj8 Caspase-3 specific unnatural amino acid peptides 4jje Caspase-3 specific unnatural amino acid peptides 4jqy Human procaspase-3, crystal form 1 4jqz Human procaspase-3, crystal form 2 4jr0 Human procaspase-3 bound to Ac-DEVD-CMK 4jr1 Human procaspase-7 bound to Ac-DEVD-CMK 4jr2 Human procaspase-7/caspase-7 heterodimer bound to Ac-DEVD-CMK 4lsz 4LSZ 4m9r Crystal structure of CED-3 4n5d Tailoring Small Molecules for an Allosteric Site on Procaspase-6: Cpd1 4n6g Tailoring Small Molecules for an Allosteric Site on Procaspase-6 4n7j Tailoring Small Molecules for an Allosteric Site on Procaspase-6 4n7m Tailoring Small Molecules for an Allosteric Site on Procaspase-6 4nbk Tailoring Small Molecules for an Allosteric Site on Procaspase-6 4nbl Tailoring Small Molecules for an Allosteric Site on Procaspase-6 4nbn Tailoring Small Molecules for an Allosteric Site on Procaspase-6 4pry 4PRY 4prz 4PRZ 4ps0 4PS0 4ps1 4PS1 4qtx 4QTX 4qty 4QTY 4qu0 4QU0 4qu5 4QU5 4qu8 4QU8 4qu9 4QU9 4qua 4QUA 4qub 4QUB 4qud 4QUD 4que 4QUE 4qug 4QUG 4quh 4QUH 4qui 4QUI 4quj 4QUJ 4qul 4QUL 4zvo 4ZVO 4zvp 4ZVP 4zvq 4ZVQ 4zvr 4ZVR 4zvs 4ZVS 4zvt 4ZVT 4zvu 4ZVU 5i9b 5I9B 5i9t 5I9T 5iab 5IAB 5iae 5IAE 5iag 5IAG 5iaj 5IAJ 5iak 5IAK 5ian 5IAN 5iar 5IAR 5ias 5IAS 5ibc 5IBC 5ibp 5IBP 5ibr 5IBR 5ic4 5IC4 5ic6 5IC6 5jft 5JFT - Links (links to other resources describing this domain)
-
BLOCKS ASPASE_HIS INTERPRO IPR015917 PROSITE CASc_DOMAIN