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1kjw

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(New page: 200px<br /><applet load="1kjw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kjw, resolution 1.8&Aring;" /> '''SH3-Guanylate Kinase ...)
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Revision as of 17:11, 20 November 2007


1kjw, resolution 1.8Å

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SH3-Guanylate Kinase Module from PSD-95

Overview

Membrane-associated guanylate kinases (MAGUKs), such as PSD-95, are, modular scaffolds that organize signaling complexes at synapses and other, cell junctions. MAGUKs contain PDZ domains, which recruit signaling, proteins, as well as a Src homology 3 (SH3) and a guanylate kinase-like, (GK) domain, implicated in scaffold oligomerization. The crystal structure, of the SH3-GK module from PSD-95 reveals that these domains form an, integrated unit: the SH3 fold comprises noncontiguous sequence elements, divided by a hinge region and the GK domain. These elements compose two, subdomains that can assemble in either an intra- or intermolecular fashion, to complete the SH3 fold. We propose a model for MAGUK oligomerization in, which complementary SH3 subdomains associate by 3D domain swapping. This, model provides a possible mechanism for ligand regulation of, oligomerization.

About this Structure

1KJW is a Single protein structure of sequence from Rattus norvegicus with SO4 as ligand. Full crystallographic information is available from OCA.

Reference

Structure of the SH3-guanylate kinase module from PSD-95 suggests a mechanism for regulated assembly of MAGUK scaffolding proteins., McGee AW, Dakoji SR, Olsen O, Bredt DS, Lim WA, Prehoda KE, Mol Cell. 2001 Dec;8(6):1291-301. PMID:11779504

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