3c35: Difference between revisions
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[[Category: Mayer, M L.]] | [[Category: Mayer, M L.]] | ||
[[Category: Membrane protein]] | [[Category: Membrane protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 25 15:14:02 2008'' | |||
Revision as of 15:14, 25 June 2008
Crystal structure of GluR5 ligand-binding core in complex with cesium at 1.97 Angstrom resolution
OverviewOverview
L-glutamate, the major excitatory neurotransmitter in the human brain, activates a family of ligand-gated ion channels, the major subtypes of which are named AMPA, kainate, and NMDA receptors. In common with many signal transduction proteins, glutamate receptors are modulated by ions and small molecules, including Ca(2+), Mg(2+), Zn(2+), protons, polyamines, and steroids. Strikingly, the activation of kainate receptors by glutamate requires the presence of both Na(+) and Cl(-) in the extracellular solution, and in the absence of these ions, receptor activity is abolished. Here, we identify the site and mechanism of action of anions. Surprisingly, we find that Cl(-) ions are essential structural components of kainate receptors. Cl(-) ions bind in a cavity formed at the interface between subunits in a dimer pair. In the absence of Cl(-), dimer stability is reduced, the rate of desensitization increases, and the fraction of receptors competent for activation by glutamate drops precipitously.
About this StructureAbout this Structure
3C35 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
Structure and mechanism of kainate receptor modulation by anions., Plested AJ, Mayer ML, Neuron. 2007 Mar 15;53(6):829-41. PMID:17359918
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