4f29

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[[Image:4f29.png|left|200px]]
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==Quisqualate bound to the ligand binding domain of GluA3i==
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<StructureSection load='4f29' size='340' side='right' caption='[[4f29]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4f29]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F29 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F29 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=QUS:(S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC+ACID'>QUS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4f1y|4f1y]], [[4f22|4f22]], [[4f2o|4f2o]], [[4f2q|4f2q]], [[4f31|4f31]]</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Glur3, Gria3, Gria3; GluA3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4f29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f29 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f29 RCSB], [http://www.ebi.ac.uk/pdbsum/4f29 PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Ligand-gated ion channels undergo conformational changes that transfer the energy of agonist binding to channel opening. Within ionotropic glutamate receptor (iGluR) subunits, this process is initiated in their bilobate ligand binding domain (LBD) where agonist binding to lobe 1 favors closure of lobe 2 around the agonist and allows formation of interlobe hydrogen bonds. AMPA receptors (GluAs) differ from other iGluRs because glutamate binding causes an aspartate-serine peptide bond in a flexible part of lobe 2 to rotate 180 degrees (flipped conformation), allowing these residues to form cross-cleft H-bonds with tyrosine and glycine in lobe 1. This aspartate also contacts the side chain of a lysine residue in the hydrophobic core of lobe 2 by a salt bridge. We investigated how the peptide flip and electrostatic contact (D655-K660) in GluA3 contribute to receptor function by examining pharmacological and structural properties with an antagonist (CNQX), a partial agonist (kainate), and two full agonists (glutamate and quisqualate) in the wildtype and two mutant receptors. Alanine substitution decreased the agonist potency of GluA3(i)-D655A and GluA3(i)-K660A receptor channels expressed in HEK293 cells and differentially affected agonist binding affinity for isolated LBDs without changing CNQX affinity. Correlations observed in the crystal structures of the mutant LBDs included the loss of the D655-K660 electrostatic contact, agonist-dependent differences in lobe 1 and lobe 2 closure, and unflipped D(A)655-S656 bonds. Glutamate-stimulated activation was slower for both mutants, suggesting that efficient energy transfer of agonist binding within the LBD of AMPA receptors requires an intact tether between the flexible peptide flip domain and the rigid hydrophobic core of lobe 2.
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The loss of an electrostatic contact unique to AMPA receptor ligand binding domain 2 slows channel activation.,Holley SM, Ahmed AH, Srinivasan J, Murthy SE, Weiland GA, Oswald RE, Nowak LM Biochemistry. 2012 May 15;51(19):4015-27. Epub 2012 May 2. PMID:22512472<ref>PMID:22512472</ref>
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{{STRUCTURE_4f29| PDB=4f29 | SCENE= }}
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===Quisqualate bound to the ligand binding domain of GluA3i===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==See Also==
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*[[Ionotropic Glutamate Receptors|Ionotropic Glutamate Receptors]]
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The line below this paragraph, {{ABSTRACT_PUBMED_22512472}}, adds the Publication Abstract to the page
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== References ==
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(as it appears on PubMed at http://www.pubmed.gov), where 22512472 is the PubMed ID number.
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<references/>
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__TOC__
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{{ABSTRACT_PUBMED_22512472}}
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</StructureSection>
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==About this Structure==
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[[4f29]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F29 OCA].
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==Reference==
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<ref group="xtra">PMID:022512472</ref><references group="xtra"/>
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Ahmed, A H.]]
[[Category: Ahmed, A H.]]

Revision as of 08:20, 5 June 2014

Quisqualate bound to the ligand binding domain of GluA3i

4f29, resolution 1.75Å

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