1KJW

SH3-Guanylate Kinase Module from PSD-95

Summary for 1KJW

• Entry DOI: 10.2210/pdb1kjw/pdb
• Descriptor: POSTSYNAPTIC DENSITY PROTEIN 95, SULFATE ION (3 entities in total)
• Functional Keywords: protein-protein interaction, scaffold, neuropeptide
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cell membrane; Peripheral membrane protein: P31016
• Total number of polymer chains: 1
• Total formula weight: 34433.49

Authors

McGee, A.W.,Dakoji, S.R.,Olsen, O.,Bredt, D.S.,Lim, W.A.,Prehoda, K.E. (deposition date: 2001-12-05, release date: 2002-01-09, Last modification date: 2024-02-14)

Primary citation

McGee, A.W.,Dakoji, S.R.,Olsen, O.,Bredt, D.S.,Lim, W.A.,Prehoda, K.E.
Structure of the SH3-Guanylate Kinase Module from PSD-95 Suggests a Mechanism for Regulated Assembly of MAGUK Scaffolding Proteins
Mol.Cell, 8:1291-1301, 2001

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 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.

PubMed: 11779504
DOI: 10.1016/S1097-2765(01)00411-7

Experimental method

X-RAY DIFFRACTION (1.8 Å)