2i3w: Difference between revisions

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[[Image:2i3w.gif|left|200px]]
{{Seed}}
[[Image:2i3w.png|left|200px]]


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{{STRUCTURE_2i3w|  PDB=2i3w  |  SCENE=  }}  
{{STRUCTURE_2i3w|  PDB=2i3w  |  SCENE=  }}  


'''Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of S729C mutant'''
===Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of S729C mutant===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_17018279}}, adds the Publication Abstract to the page
(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]
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 g729c mutant]]
[[Category: Ionotropic glutamate receptor ligand binding core s1s2 g729c mutant]]
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