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

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)