1pau

From Proteopedia

Revision as of 16:35, 12 November 2007

CRYSTAL STRUCTURE OF THE COMPLEX OF APOPAIN WITH THE TETRAPEPTIDE ALDEHYDE INHIBITOR AC-DEVD-CHO

Overview

Cysteine proteases related to mammalian interleukin-1 beta converting, enzyme (ICE) and to its Caenorhabditis elegans homologue, CED-3, play a, critical role in the biochemical events that culminate in apoptosis. We, have determined the three-dimensional structure of a complex of the human, CED-3 homologue CPP32/apopain with a potent tetrapeptide-aldehyde, inhibitor. The protein resembles ICE in overall structure, but its S4, subsite is strikingly different in size and chemical composition. These, differences account for the variation in specificity between the ICE- and, CED-3-related proteases and enable the design of specific inhibitors that, can probe the physiological functions of the proteins and disease states, with which they are associated.

About this Structure

1PAU is a Protein complex structure of sequences from Homo sapiens with ACE as ligand. The following page contains interesting information on the relation of 1PAU with [Caspases]. Structure known Active Sites: S1, S2, S3 and S4. Full crystallographic information is available from OCA.

Reference

The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis., Rotonda J, Nicholson DW, Fazil KM, Gallant M, Gareau Y, Labelle M, Peterson EP, Rasper DM, Ruel R, Vaillancourt JP, Thornberry NA, Becker JW, Nat Struct Biol. 1996 Jul;3(7):619-25. PMID:8673606

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