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| [[Image:1t3e.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1t3e| PDB=1t3e | SCENE= }} | | {{STRUCTURE_1t3e| PDB=1t3e | SCENE= }} |
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| '''Structural basis of dynamic glycine receptor clustering'''
| | ===Structural basis of dynamic glycine receptor clustering=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15201864}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15201864 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15201864}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Timmins, J.]] | | [[Category: Timmins, J.]] |
| [[Category: Alfa-beta]] | | [[Category: Alfa-beta]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:28:07 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:16:22 2008'' |
