Ontology highlight
ABSTRACT:
SUBMITTER: Sola M
PROVIDER: S-EPMC449768 | biostudies-literature | 2004 Jul
REPOSITORIES: biostudies-literature
Sola Maria M Bavro Vassiliy N VN Timmins Joanna J Franz Thomas T Ricard-Blum Sylvie S Schoehn Guy G Ruigrok Rob W H RW Paarmann Ingo I Saiyed Taslimarif T O'Sullivan Gregory A GA Schmitt Bertram B Betz Heinrich H Weissenhorn Winfried W
The EMBO journal 20040617 13
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 ...[more]