1ocs

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Revision as of 20:05, 29 October 2007

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spinqualitylabelsall models 1ocs, resolution 2.03Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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]. 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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