1ocs

From Proteopedia

Revision as of 13:45, 30 October 2007

CRYSTAL STRUCTURE OF THE YEAST PX-DOAMIN PROTEIN GRD19P (SORTING NEXIN3) COMPLEXED TO PHOSPHATIDYLINOSYTOL-3-PHOSPHATE.

Overview

Phox homology (PX) domains have been recently identified in a number of, different proteins and are involved in various cellular functions such as, vacuolar targeting and membrane protein trafficking. It was shown that, these modules of about 130 amino acids specifically binding to, phosphoinositides and that this interaction is crucial for their cellular, function. The yeast genome contains 17 PX domain proteins. One of these, Grd19p, is involved in the localization of the late Golgi membrane, proteins DPAP A and Kex2p. Grd19p consists of the PX domain with 30 extra, residues at the N-terminal and is homologous to the functionally, characterized human sorting nexin protein SNX3. We determined the 2.0 A, crystal structure of Grd19p in the free form and in complex with, ... [(full description)]

About this Structure

1OCS is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with GOL as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Crystal structure of the yeast Phox homology (PX) domain protein Grd19p complexed to phosphatidylinositol-3-phosphate., Zhou CZ, de La Sierra-Gallay IL, Quevillon-Cheruel S, Collinet B, Minard P, Blondeau K, Henckes G, Aufrere R, Leulliot N, Graille M, Sorel I, Savarin P, de la Torre F, Poupon A, Janin J, van Tilbeurgh H, J Biol Chem. 2003 Dec 12;278(50):50371-6. Epub 2003 Sep 26. PMID:14514667

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