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Title | Structure of the SH3-guanylate kinase module from PSD-95 suggests a mechanism for regulated assembly of MAGUK scaffolding proteins. |
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Journal, issue, pages | Mol Cell, Vol. 8, Issue 6, Page 1291-1301, Year 2001 |
Publish date | Jan 16, 2002 |
Authors | A W McGee / S R Dakoji / O Olsen / D S Bredt / W A Lim / K E Prehoda / |
PubMed Abstract | 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. |
External links | Mol Cell / PubMed:11779504 |
Methods | X-ray diffraction |
Resolution | 1.8 Å |
Structure data | PDB-1kjw: |
Chemicals | ChemComp-SO4: ChemComp-HOH: |
Source |
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Keywords | NEUROPEPTIDE / PROTEIN-PROTEIN INTERACTION / SCAFFOLD |