2qs1: Difference between revisions
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<StructureSection load='2qs1' size='340' side='right'caption='[[2qs1]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='2qs1' size='340' side='right'caption='[[2qs1]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2qs1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2qs1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QS1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QS1 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=UB1:3-({3-[(2S)-2-AMINO-2-CARBOXYETHYL]-5-METHYL-2,6-DIOXO-3,6-DIHYDROPYRIMIDIN-1(2H)-YL}METHYL)-4,5-DIBROMOTHIOPHENE-2-CARBOXYLIC+ACID'>UB1</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=UB1:3-({3-[(2S)-2-AMINO-2-CARBOXYETHYL]-5-METHYL-2,6-DIOXO-3,6-DIHYDROPYRIMIDIN-1(2H)-YL}METHYL)-4,5-DIBROMOTHIOPHENE-2-CARBOXYLIC+ACID'>UB1</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qs1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qs1 OCA], [https://pdbe.org/2qs1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qs1 RCSB], [https://www.ebi.ac.uk/pdbsum/2qs1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qs1 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qs1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qs1 OCA], [https://pdbe.org/2qs1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qs1 RCSB], [https://www.ebi.ac.uk/pdbsum/2qs1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qs1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/GRIK1_RAT GRIK1_RAT] Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. May be involved in the transmission of light information from the retina to the hypothalamus.<ref>PMID:16540562</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Rattus norvegicus]] | ||
[[Category: | [[Category: Alushin GM]] | ||
[[Category: | [[Category: Jane DE]] | ||
[[Category: | [[Category: Mayer ML]] | ||
Latest revision as of 14:39, 30 August 2023
Crystal structure of the GluR5 ligand binding core dimer in complex with UBP315 at 1.80 Angstroms resolutionCrystal structure of the GluR5 ligand binding core dimer in complex with UBP315 at 1.80 Angstroms resolution
Structural highlights
FunctionGRIK1_RAT Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. May be involved in the transmission of light information from the retina to the hypothalamus.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe availability of crystal structures for the ligand binding domains of ionotropic glutamate receptors, combined with their key role in synaptic function in the normal and diseased brain, offers a unique selection of targets for pharmaceutical research compared to other drug targets for which the atomic structure of the ligand binding site is not known. Currently only a few antagonist structures have been solved, and these reveal ligand specific conformational changes that hinder rational drug design. Here we report high resolution crystal structures for three kainate receptor GluK1 antagonist complexes which reveal new and unexpected modes of binding, highlighting the continued need for experimentally determined receptor-ligand complexes. Binding site and ligand flexibility revealed by high resolution crystal structures of GluK1 competitive antagonists.,Alushin GM, Jane D, Mayer ML Neuropharmacology. 2011 Jan;60(1):126-34. Epub 2010 Jun 15. PMID:20558186[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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