2i3v

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[[Image:2i3v.gif|left|200px]]
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{{STRUCTURE_2i3v| PDB=2i3v | SCENE= }}
{{STRUCTURE_2i3v| PDB=2i3v | SCENE= }}
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'''Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of G725C mutant'''
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===Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of G725C mutant===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_17018279}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 17018279 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17018279}}
==About this Structure==
==About this Structure==
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/17018279 17018279]
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:[http://www.ncbi.nlm.nih.gov/pubmed/17018279 17018279]
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Probing the ligand binding domain of the GluR2 receptor by proteolysis and deletion mutagenesis defines domain boundaries and yields a crystallizable construct., Chen GQ, Sun Y, Jin R, Gouaux E, Protein Sci. 1998 Dec;7(12):2623-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9865957 9865957]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Jasti, J.]]
[[Category: Jasti, J.]]
[[Category: Ionotropic glutamate receptor ligand binding core s1s2 g725c mutant]]
[[Category: Ionotropic glutamate receptor ligand binding core s1s2 g725c mutant]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:02:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:57:26 2008''

Revision as of 03:57, 29 July 2008

Image:2i3v.png

Template:STRUCTURE 2i3v

Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of G725C mutant

Template:ABSTRACT PUBMED 17018279

About this Structure

2I3V is a Single protein structure of sequence from Rattus norvegicus. 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

Probing the ligand binding domain of the GluR2 receptor by proteolysis and deletion mutagenesis defines domain boundaries and yields a crystallizable construct., Chen GQ, Sun Y, Jin R, Gouaux E, Protein Sci. 1998 Dec;7(12):2623-30. PMID:9865957

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