2f34

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{{STRUCTURE_2f34| PDB=2f34 | SCENE= }}
{{STRUCTURE_2f34| PDB=2f34 | SCENE= }}
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'''Crystal Structure of the GluR5 Ligand Binding Core Dimer with UBP310 At 1.74 Angstroms Resolution'''
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===Crystal Structure of the GluR5 Ligand Binding Core Dimer with UBP310 At 1.74 Angstroms Resolution===
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==Overview==
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Glutamate receptor (GluR) ion channels mediate fast synaptic transmission in the mammalian CNS. Numerous crystallographic studies, the majority on the GluR2-subtype AMPA receptor, have revealed the structural basis for binding of subtype-specific agonists. In contrast, because there are far fewer antagonist-bound structures, the mechanisms for antagonist binding are much less well understood, particularly for kainate receptors that exist as multiple subtypes with a distinct biology encoded by the GluR5-7, KA1, and KA2 genes. We describe here high-resolution crystal structures for the GluR5 ligand-binding core complex with UBP302 and UBP310, novel GluR5-selective antagonists. The crystal structures reveal the structural basis for the high selectivity for GluR5 observed in radiolabel displacement assays for the isolated ligand binding cores of the GluR2, GluR5, and GluR6 subunits and during inhibition of glutamate-activated currents in studies on full-length ion channels. The antagonists bind via a novel mechanism and do not form direct contacts with the E723 side chain as occurs in all previously solved AMPA and kainate receptor agonist and antagonist complexes. This results from a hyperextension of the ligand binding core compared with previously solved structures. As a result, in dimer assemblies, there is a 22 A extension of the ion channel linkers in the transition from antagonist- to glutamate-bound forms. This large conformational change is substantially different from that described for AMPA receptors, was not possible to predict from previous work, and suggests that glutamate receptors are capable of much larger movements than previously thought.
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(as it appears on PubMed at http://www.pubmed.gov), where 16540562 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16540562}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Crystal structures of the kainate receptor GluR5 ligand binding core dimer with novel GluR5-selective antagonists., Mayer ML, Ghosal A, Dolman NP, Jane DE, J Neurosci. 2006 Mar 15;26(11):2852-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16540562 16540562]
Crystal structures of the kainate receptor GluR5 ligand binding core dimer with novel GluR5-selective antagonists., Mayer ML, Ghosal A, Dolman NP, Jane DE, J Neurosci. 2006 Mar 15;26(11):2852-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16540562 16540562]
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Crystal structures of the GluR5 and GluR6 ligand binding cores: molecular mechanisms underlying kainate receptor selectivity., Mayer ML, Neuron. 2005 Feb 17;45(4):539-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15721240 15721240]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Mayer, M L.]]
[[Category: Mayer, M L.]]
[[Category: Membrane protein]]
[[Category: Membrane protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:24:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:06:06 2008''

Revision as of 21:06, 28 July 2008

Image:2f34.png

Template:STRUCTURE 2f34

Crystal Structure of the GluR5 Ligand Binding Core Dimer with UBP310 At 1.74 Angstroms Resolution

Template:ABSTRACT PUBMED 16540562

About this Structure

2F34 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Crystal structures of the kainate receptor GluR5 ligand binding core dimer with novel GluR5-selective antagonists., Mayer ML, Ghosal A, Dolman NP, Jane DE, J Neurosci. 2006 Mar 15;26(11):2852-61. PMID:16540562

Crystal structures of the GluR5 and GluR6 ligand binding cores: molecular mechanisms underlying kainate receptor selectivity., Mayer ML, Neuron. 2005 Feb 17;45(4):539-52. PMID:15721240

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