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-Structure paper
タイトル | Structure of the SH3-guanylate kinase module from PSD-95 suggests a mechanism for regulated assembly of MAGUK scaffolding proteins. |
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ジャーナル・号・ページ | Mol Cell, Vol. 8, Issue 6, Page 1291-1301, Year 2001 |
掲載日 | 2002年1月16日 |
著者 | A W McGee / S R Dakoji / O Olsen / D S Bredt / W A Lim / K E Prehoda / |
PubMed 要旨 | 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 ...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. |
リンク | Mol Cell / PubMed:11779504 |
手法 | X線回折 |
解像度 | 1.8 Å |
構造データ | PDB-1kjw: |
化合物 | ChemComp-SO4: ChemComp-HOH: |
由来 |
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キーワード | NEUROPEPTIDE / PROTEIN-PROTEIN INTERACTION (タンパク質間相互作用) / SCAFFOLD (足場) |