1t3e
From Proteopedia
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'''Structural basis of dynamic glycine receptor clustering''' | '''Structural basis of dynamic glycine receptor clustering''' | ||
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[[Category: Sullivan, G A.O.]] | [[Category: Sullivan, G A.O.]] | ||
[[Category: Timmins, J.]] | [[Category: Timmins, J.]] | ||
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Revision as of 06:28, 3 May 2008
Structural basis of dynamic glycine receptor clustering
Overview
Gephyrin is a bi-functional modular protein involved in molybdenum cofactor biosynthesis and in postsynaptic clustering of inhibitory glycine receptors (GlyRs). Here, we show that full-length gephyrin is a trimer and that its proteolysis in vitro causes the spontaneous dimerization of its C-terminal region (gephyrin-E), which binds a GlyR beta-subunit-derived peptide with high and low affinity. The crystal structure of the tetra-domain gephyrin-E in complex with the beta-peptide bound to domain IV indicates how membrane-embedded GlyRs may interact with subsynaptic gephyrin. In vitro, trimeric full-length gephyrin forms a network upon lowering the pH, and this process can be reversed to produce stable full-length dimeric gephyrin. Our data suggest a mechanism by which induced conformational transitions of trimeric gephyrin may generate a reversible postsynaptic scaffold for GlyR recruitment, which allows for dynamic receptor movement in and out of postsynaptic GlyR clusters, and thus for synaptic plasticity.
About this Structure
1T3E is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structural basis of dynamic glycine receptor clustering by gephyrin., Sola M, Bavro VN, Timmins J, Franz T, Ricard-Blum S, Schoehn G, Ruigrok RW, Paarmann I, Saiyed T, O'Sullivan GA, Schmitt B, Betz H, Weissenhorn W, EMBO J. 2004 Jul 7;23(13):2510-9. Epub 2004 Jun 17. PMID:15201864 Page seeded by OCA on Sat May 3 09:28:07 2008
