1i51 | pdb_00001i51
CRYSTAL STRUCTURE OF CASPASE-7 COMPLEXED WITH XIAP
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Overview
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.
Disease
Known diseases associated with this structure: Lymphoproliferative syndrome, X-linked, 2 OMIM:[300079]
About this Structure
1I51 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis of caspase-7 inhibition by XIAP., Chai J, Shiozaki E, Srinivasula SM, Wu Q, Datta P, Alnemri ES, Shi Y, Cell. 2001 Mar 9;104(5):769-80. PMID:11257230
Page seeded by OCA on Thu Feb 21 13:08:06 2008
