2ojt

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(New page: 200px<br /><applet load="2ojt" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ojt, resolution 1.95&Aring;" /> '''Structure and mechan...)
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==Overview==
==Overview==
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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.
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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 Structure==
==About this Structure==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Mayer, M.L.]]
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[[Category: Mayer, M L.]]
[[Category: 1PE]]
[[Category: 1PE]]
[[Category: BR]]
[[Category: BR]]
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[[Category: membrane protein]]
[[Category: membrane protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 21:12:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:19:14 2008''

Revision as of 16:19, 21 February 2008


2ojt, resolution 1.95Å

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Structure and mechanism of kainate receptor modulation by anions

Overview

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 Structure

2OJT is a Single protein structure of sequence from Rattus norvegicus with , and as ligands. Full crystallographic information is available from OCA.

Reference

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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