1k86

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spinqualitylabelsall models 1k86, resolution 2.6Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of caspase-7

Overview

Apoptosis is primarily executed by active caspases, which are derived from, the inactive procaspase zymogens through proteolytic cleavage. Here we, report the crystal structures of a caspase zymogen, procaspase-7, and an, active caspase-7 without any bound inhibitors. Compared to the, inhibitor-bound caspase-7, procaspase-7 zymogen exhibits significant, structural differences surrounding the catalytic cleft, which precludes, the formation of a productive conformation. Proteolytic cleavage between, the large and small subunits allows rearrangement of essential loops in, the active site, priming active caspase-7 for inhibitor/substrate binding., Strikingly, binding by inhibitors causes a 180 degrees flipping of the N, terminus in the small subunit, which interacts with and stabilizes the, catalytic cleft. These analyses reveal the structural mechanisms of, caspase activation and demonstrate that the inhibitor/substrate binding is, a process of induced fit.

About this Structure

1K86 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of a procaspase-7 zymogen: mechanisms of activation and substrate binding., Chai J, Wu Q, Shiozaki E, Srinivasula SM, Alnemri ES, Shi Y, Cell. 2001 Nov 2;107(3):399-407. PMID:11701129

Page seeded by OCA on Mon Nov 12 17:48:10 2007