1p1u

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{{STRUCTURE_1p1u| PDB=1p1u | SCENE= }}
{{STRUCTURE_1p1u| PDB=1p1u | SCENE= }}
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'''Crystal structure of the GluR2 ligand-binding core (S1S2J) L650T mutant in complex with AMPA (ammonium sulfate crystal form)'''
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===Crystal structure of the GluR2 ligand-binding core (S1S2J) L650T mutant in complex with AMPA (ammonium sulfate crystal form)===
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==Overview==
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The (S)-2-amino-3-(3-hydroxy-5-methyl-4-isoxazole) propionic acid (AMPA) receptor discriminates between agonists in terms of binding and channel gating; AMPA is a high-affinity full agonist, whereas kainate is a low-affinity partial agonist. Although there is extensive literature on the functional characterization of partial agonist activity in ion channels, structure-based mechanisms are scarce. Here we investigate the role of Leu-650, a binding cleft residue conserved among AMPA receptors, in maintaining agonist specificity and regulating agonist binding and channel gating by using physiological, x-ray crystallographic, and biochemical techniques. Changing Leu-650 to Thr yields a receptor that responds more potently and efficaciously to kainate and less potently and efficaciously to AMPA relative to the WT receptor. Crystal structures of the Leu-650 to Thr mutant reveal an increase in domain closure in the kainate-bound state and a partially closed and a fully closed conformation in the AMPA-bound form. Our results indicate that agonists can induce a range of conformations in the GluR2 ligand-binding core and that domain closure is directly correlated to channel activation. The partially closed, AMPA-bound conformation of the L650T mutant likely captures the structure of an agonist-bound, inactive state of the receptor. Together with previously solved structures, we have determined a mechanism of agonist binding and subsequent conformational rearrangements.
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(as it appears on PubMed at http://www.pubmed.gov), where 12730367 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12730367}}
==About this Structure==
==About this Structure==
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[[Category: Ionotropic glutamate receptor]]
[[Category: Ionotropic glutamate receptor]]
[[Category: Ligand-binding domain]]
[[Category: Ligand-binding domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:34:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:03:24 2008''

Revision as of 16:03, 27 July 2008

Image:1p1u.png

Template:STRUCTURE 1p1u

Crystal structure of the GluR2 ligand-binding core (S1S2J) L650T mutant in complex with AMPA (ammonium sulfate crystal form)

Template:ABSTRACT PUBMED 12730367

About this Structure

1P1U is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes., Armstrong N, Mayer M, Gouaux E, Proc Natl Acad Sci U S A. 2003 May 13;100(10):5736-41. Epub 2003 May 2. PMID:12730367

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