1m4m

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(New page: 200px<br /><applet load="1m4m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m4m, resolution 2.80&Aring;" /> '''Mouse Survivin'''<br...)
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Revision as of 19:01, 20 November 2007


1m4m, resolution 2.80Å

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Mouse Survivin

Overview

The coupling of apoptosis (programmed cell death) to the cell division, cycle is essential for homeostasis and genomic integrity. Here, we report, the crystal structure of survivin, an inhibitor of apoptosis, which has, been implicated in both control of cell death and regulation of cell, division. In addition to a conserved N-terminal Zn finger baculovirus IAP, repeat, survivin forms a dimer through a symmetric interaction with an, intermolecularly bound Zn atom located along the molecular dyad axis. The, interaction of the dimer-related C-terminal alpha helices forms an, extended surface of approximately 70 A in length. Mutagenesis analysis, revealed that survivin dimerization and an extended negatively charged, surface surrounding Asp-71 are required to counteract apoptosis and, preserve ploidy. These findings may provide a structural basis for a dual, role of survivin in inhibition of apoptosis and regulation of cell, division.

About this Structure

1M4M is a Single protein structure of sequence from Mus musculus with ZN as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure and mutagenic analysis of the inhibitor-of-apoptosis protein survivin., Muchmore SW, Chen J, Jakob C, Zakula D, Matayoshi ED, Wu W, Zhang H, Li F, Ng SC, Altieri DC, Mol Cell. 2000 Jul;6(1):173-82. PMID:10949038

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