1few

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CRYSTAL STRUCTURE OF SMAC/DIABLO

Overview

Apoptosis (programmed cell death), an essential process in the development, and homeostasis of metazoans, is carried out by caspases. The, mitochondrial protein Smac/DIABLO performs a critical function in, apoptosis by eliminating the inhibitory effect of IAPs (inhibitor of, apoptosis proteins) on caspases. Here we show that Smac/DIABLO promotes, not only the proteolytic activation of procaspase-3 but also the enzymatic, activity of mature caspase-3, both of which depend upon its ability to, interact physically with IAPs. The crystal structure of Smac/DIABLO at 2.2, A resolution reveals that it homodimerizes through an extensive, hydrophobic interface. Missense mutations inactivating this dimeric, interface significantly compromise the function of Smac/DIABLO. As in the, Drosophila proteins Reaper, Grim and Hid, the amino-terminal amino acids, of Smac/DIABLO are indispensable for its function, and a seven-residue, peptide derived from the amino terminus promotes procaspase-3 activation, in vitro. These results establish an evolutionarily conserved structural, and biochemical basis for the activation of apoptosis by Smac/DIABLO.

About this Structure

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

Reference

Structural and biochemical basis of apoptotic activation by Smac/DIABLO., Chai J, Du C, Wu JW, Kyin S, Wang X, Shi Y, Nature. 2000 Aug 24;406(6798):855-62. PMID:10972280

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