1I51

CRYSTAL STRUCTURE OF CASPASE-7 COMPLEXED WITH XIAP

Summary for 1I51

• Entry DOI: 10.2210/pdb1i51/pdb
• Descriptor: CASPASE-7 SUBUNIT P20, CASPASE-7 SUBUNIT P11, X-LINKED INHIBITOR OF APOPTOSIS PROTEIN (3 entities in total)
• Functional Keywords: protease, caspase, iap, apoptosis, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: P55210 P55210 P98170
• Total number of polymer chains: 6
• Total formula weight: 84924.08

Authors

Chai, J.,Shi, Y. (deposition date: 2001-02-23, release date: 2002-02-23, Last modification date: 2023-08-09)

Primary citation

Chai, J.,Shiozaki, E.,Srinivasula, S.M.,Wu, Q.,Datta, P.,Alnemri, E.S.,Shi, Y.,Dataa, P.
Structural basis of caspase-7 inhibition by XIAP.
Cell(Cambridge,Mass.), 104:769-780, 2001

PubMed Abstract: The inhibitor of apoptosis (IAP) proteins suppress cell death by inhibiting the catalytic activity of caspases. Here we present the crystal structure of caspase-7 in complex with a potent inhibitory fragment from XIAP at 2.45 A resolution. An 18-residue XIAP peptide binds the catalytic groove of caspase-7, making extensive contacts to the residues that are essential for its catalytic activity. Strikingly, despite a reversal of relative orientation, a subset of interactions between caspase-7 and XIAP closely resemble those between caspase-7 and its tetrapeptide inhibitor DEVD-CHO. Our biochemical and structural analyses reveal that the BIR domains are dispensable for the inhibition of caspase-3 and -7. This study provides a structural basis for the design of the next-generation caspase inhibitors.

PubMed: 11257230
DOI: 10.1016/S0092-8674(01)00272-0

Experimental method

X-RAY DIFFRACTION (2.45 Å)