1QDU
CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-8 WITH THE TRIPEPTIDE KETONE INHIBITOR ZEVD-DCBMK
Summary for 1QDU
Entry DOI | 10.2210/pdb1qdu/pdb |
Related PRD ID | PRD_000295 |
Descriptor | CASPASE-8 ALPHA-CHAIN, CASPASE-8 BETA-CHAIN, PHQ-GLU-VAL-ASP-DICHLOROMETHYLKETONE INHIBITOR, ... (4 entities in total) |
Functional Keywords | apoptosis, cysteine protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
Biological source | Homo sapiens (human) More |
Cellular location | Cytoplasm: Q14790 Q14790 |
Total number of polymer chains | 18 |
Total formula weight | 168899.98 |
Authors | Blanchard, H.,Grutter, M.G. (deposition date: 1999-07-10, release date: 2000-07-10, Last modification date: 2024-04-03) |
Primary citation | Blanchard, H.,Kodandapani, L.,Mittl, P.R.,Marco, S.D.,Krebs, J.F.,Wu, J.C.,Tomaselli, K.J.,Grutter, M.G. The three-dimensional structure of caspase-8: an initiator enzyme in apoptosis. Structure Fold.Des., 7:1125-1133, 1999 Cited by PubMed Abstract: In the initial stages of Fas-mediated apoptosis the cysteine protease caspase-8 is recruited to the cell receptor as a zymogen (procaspase-8) and is incorporated into the death-signalling complex. Procaspase-8 is subsequently activated leading to a cascade of proteolytic events, one of them being the activation of caspase-3, and ultimately resulting in cell destruction. Variations in the substrate specificity of different caspases have been reported. PubMed: 10508784DOI: 10.1016/S0969-2126(99)80179-8 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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