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TitleStructure of the SH3-guanylate kinase module from PSD-95 suggests a mechanism for regulated assembly of MAGUK scaffolding proteins.
Journal, issue, pagesMol Cell, Vol. 8, Issue 6, Page 1291-1301, Year 2001
Publish dateJan 16, 2002
AuthorsA W McGee / S R Dakoji / O Olsen / D S Bredt / W A Lim / K E Prehoda /
PubMed AbstractMembrane-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 linksMol Cell / PubMed:11779504
MethodsX-ray diffraction
Resolution1.8 Å
Structure data

PDB-1kjw:
SH3-Guanylate Kinase Module from PSD-95
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • rattus norvegicus (Norway rat)
KeywordsNEUROPEPTIDE / PROTEIN-PROTEIN INTERACTION / SCAFFOLD

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