2i3v
From Proteopedia
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Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of G725C mutant
Overview
The canonical conformational states occupied by most ligand-gated ion channels, and many cell-surface receptors, are the resting, activated, and desensitized states. While the resting and activated states of multiple receptors are well characterized, elaboration of the structural properties of the desensitized state, a state that is by definition inactive, has proven difficult. Here we use electrical, chemical, and crystallographic experiments on the AMPA-sensitive GluR2 receptor, defining the conformational rearrangements of the agonist binding cores that occur upon desensitization of this ligand-gated ion channel. These studies demonstrate that desensitization involves the rupture of an extensive interface between domain 1 of 2-fold related glutamate-binding core subunits, compensating for the ca. 21 degrees of domain closure induced by glutamate binding. The rupture of the domain 1 interface allows the ion channel to close and thereby provides a simple explanation to the long-standing question of how agonist binding is decoupled from ion channel gating upon receptor desensitization.
About this Structure
2I3V is a Single protein structure of sequence from Rattus norvegicus with and as ligands. Full crystallographic information is available from OCA.
Reference
Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor., Armstrong N, Jasti J, Beich-Frandsen M, Gouaux E, Cell. 2006 Oct 6;127(1):85-97. PMID:17018279
Page seeded by OCA on Thu Feb 21 17:48:45 2008
