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1QDU

CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-8 WITH THE TRIPEPTIDE KETONE INHIBITOR ZEVD-DCBMK

Summary for 1QDU
Entry DOI10.2210/pdb1qdu/pdb
Related PRD IDPRD_000295
DescriptorCASPASE-8 ALPHA-CHAIN, CASPASE-8 BETA-CHAIN, PHQ-GLU-VAL-ASP-DICHLOROMETHYLKETONE INHIBITOR, ... (4 entities in total)
Functional Keywordsapoptosis, cysteine protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceHomo sapiens (human)
More
Cellular locationCytoplasm: Q14790 Q14790
Total number of polymer chains18
Total formula weight168899.98
Authors
Blanchard, H.,Grutter, M.G. (deposition date: 1999-07-10, release date: 2000-07-10, Last modification date: 2024-11-13)
Primary citationBlanchard, 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: 10508784
DOI: 10.1016/S0969-2126(99)80179-8
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

227933

數據於2024-11-27公開中

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