5ikb: Difference between revisions
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==Crystal structure of the kainate receptor GluK4 ligand binding domain in complex with kainate== | ==Crystal structure of the kainate receptor GluK4 ligand binding domain in complex with kainate== | ||
<StructureSection load='5ikb' size='340' side='right' caption='[[5ikb]], [[Resolution|resolution]] 2.05Å' scene=''> | <StructureSection load='5ikb' size='340' side='right'caption='[[5ikb]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ikb]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IKB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IKB FirstGlance]. <br> | <table><tr><td colspan='2'>[[5ikb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IKB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IKB FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=KAI:3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE'>KAI</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=KAI:3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE'>KAI</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Grik4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ikb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ikb OCA], [http://pdbe.org/5ikb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ikb RCSB], [http://www.ebi.ac.uk/pdbsum/5ikb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ikb ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ikb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ikb OCA], [http://pdbe.org/5ikb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ikb RCSB], [http://www.ebi.ac.uk/pdbsum/5ikb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ikb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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</div> | </div> | ||
<div class="pdbe-citations 5ikb" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5ikb" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ionotropic Glutamate Receptors|Ionotropic Glutamate Receptors]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Buffalo rat]] | |||
[[Category: Large Structures]] | |||
[[Category: Frydenvang, K]] | [[Category: Frydenvang, K]] | ||
[[Category: Kastrup, J S]] | [[Category: Kastrup, J S]] | ||
Revision as of 09:53, 27 March 2019
Crystal structure of the kainate receptor GluK4 ligand binding domain in complex with kainateCrystal structure of the kainate receptor GluK4 ligand binding domain in complex with kainate
Structural highlights
Function[GRIK4_RAT] Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds kainate > quisqualate > glutamate >> AMPA. Publication Abstract from PubMedIonotropic glutamate receptors play a key role in fast neurotransmission in the CNS and have been linked to several neurological diseases and disorders. One subfamily is the kainate receptors, which are grouped into low-affinity (GluK1-3) and high-affinity (GluK4-5) receptors based on their affinity for kainate. Although structures of the ligand-binding domain (LBD) of all low-affinity kainate receptors have been reported, no structures of the high-affinity receptor subunits are available. Here, we present the X-ray structure of GluK4-LBD with kainate at 2.05 A resolution, together with thermofluor and radiolabel binding affinity data. Whereas binding-site residues in GluK4 are most similar to the AMPA receptor subfamily, the domain closure and D1-D2 interlobe contacts induced by kainate are similar to the low-affinity kainate receptor GluK1. These observations provide a likely explanation for the high binding affinity of kainate at GluK4-LBD. The Structure of a High-Affinity Kainate Receptor: GluK4 Ligand-Binding Domain Crystallized with Kainate.,Kristensen O, Kristensen LB, Mollerud S, Frydenvang K, Pickering DS, Kastrup JS Structure. 2016 Sep 6;24(9):1582-9. doi: 10.1016/j.str.2016.06.019. Epub 2016 Aug, 11. PMID:27524200[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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