1i4o

From Proteopedia

Revision as of 15:19, 12 November 2007

CRYSTAL STRUCTURE OF THE XIAP/CASPASE-7 COMPLEX

Overview

The inhibitor of apoptosis proteins (IAPs) represent the only endogenous, caspase inhibitors and are characterized by the presence of baculoviral, IAP repeats (BIRs). Here, we report the crystal structure of the complex, between human caspase-7 and XIAP (BIR2 and the proceeding linker). The, structure surprisingly reveals that the linker is the only contacting, element for the caspase, while the BIR2 domain is invisible in the, crystal. The linker interacts with and blocks the substrate groove of the, caspase in a backward fashion, distinct from substrate recognition., Structural analyses suggest that the linker is the energetic and, specificity determinant of the interaction. Further biochemical, characterizations clearly establish that the linker harbors the major, energetic determinant, while the BIR2 domain serves as a regulatory, element for caspase binding and Smac neutralization.

Disease

Known diseases associated with this structure: Lymphoproliferative syndrome, X-linked, 2 OMIM:[300079]

About this Structure

1I4O is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis of caspase inhibition by XIAP: differential roles of the linker versus the BIR domain., Huang Y, Park YC, Rich RL, Segal D, Myszka DG, Wu H, Cell. 2001 Mar 9;104(5):781-90. PMID:11257231

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