1PAU
Crystal structure of the complex of apopain with the tetrapeptide aldehyde inhibitor AC-DEVD-CHO
Summary for 1PAU
| Entry DOI | 10.2210/pdb1pau/pdb |
| Related PRD ID | PRD_000422 |
| Descriptor | APOPAIN, ACE-ASP-GLU-VAL-ASJ, ... (4 entities in total) |
| Functional Keywords | cysteine protease, caspase-3, apopain, cpp32, yama, protease-inhibitor complex, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Homo sapiens (human) More |
| Cellular location | Cytoplasm: P42574 P42574 |
| Total number of polymer chains | 3 |
| Total formula weight | 29038.99 |
| Authors | Rotonda, J.,Becker, J.W. (deposition date: 1996-06-06, release date: 1997-07-07, Last modification date: 2023-08-09) |
| Primary citation | Rotonda, J.,Nicholson, D.W.,Fazil, K.M.,Gallant, M.,Gareau, Y.,Labelle, M.,Peterson, E.P.,Rasper, D.M.,Ruel, R.,Vaillancourt, J.P.,Thornberry, N.A.,Becker, J.W. The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis. Nat.Struct.Biol., 3:619-625, 1996 Cited by PubMed Abstract: Cysteine proteases related to mammalian interleukin-1 beta converting enzyme (ICE) and to its Caenorhabditis elegans homologue, CED-3, play a critical role in the biochemical events that culminate in apoptosis. We have determined the three-dimensional structure of a complex of the human CED-3 homologue CPP32/apopain with a potent tetrapeptide-aldehyde inhibitor. The protein resembles ICE in overall structure, but its S4 subsite is strikingly different in size and chemical composition. These differences account for the variation in specificity between the ICE- and CED-3-related proteases and enable the design of specific inhibitors that can probe the physiological functions of the proteins and disease states with which they are associated. PubMed: 8673606DOI: 10.1038/nsb0796-619 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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