2atx

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(New page: 200px<br /> <applet load="2atx" size="450" color="white" frame="true" align="right" spinBox="true" caption="2atx, resolution 2.65&Aring;" /> '''Crystal Structure o...)
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Revision as of 18:48, 12 November 2007


2atx, resolution 2.65Å

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Crystal Structure of the TC10 GppNHp complex

Overview

The specific and rapid formation of protein complexes is essential for, diverse cellular processes such as remodeling of actin filaments in, response to the interaction between Rho GTPases and the Wiskott-Aldrich, syndrome proteins (WASp and N-WASp). Although Cdc42, TC10, and other, members of the Rho family have been implicated in binding to and, activating the WAS proteins, the exact nature of such a protein-protein, recognition process has remained obscure. Here, we describe a mechanism, that ensures rapid and selective long-range Cdc42-WASp recognition. The, crystal structure of TC10, together with mutational and bioinformatic, analyses, proved that the basic region of WASp and two unique glutamates, in Cdc42 generate favorable electrostatic steering forces that control the, accelerated WASp-Cdc42 association reaction. This process is a, prerequisite for WASp activation and a critical step in temporal, regulation and integration of WASp-mediated cellular responses.

About this Structure

2ATX is a Single protein structure of sequence from Homo sapiens with MG and GNP as ligands. Active as Small monomeric GTPase, with EC number 3.6.5.2 Full crystallographic information is available from OCA.

Reference

An electrostatic steering mechanism of Cdc42 recognition by Wiskott-Aldrich syndrome proteins., Hemsath L, Dvorsky R, Fiegen D, Carlier MF, Ahmadian MR, Mol Cell. 2005 Oct 28;20(2):313-24. PMID:16246732

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