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| | <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 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> | + | <table><tr><td colspan='2'>[[5ikb]] is a 1 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=5IKB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=KAI:3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE'>KAI</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=5ikb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ikb OCA], [https://pdbe.org/5ikb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ikb RCSB], [https://www.ebi.ac.uk/pdbsum/5ikb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ikb ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GRIK4_RAT 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. | + | [https://www.uniprot.org/uniprot/GRIK4_RAT 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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Ionotropic Glutamate Receptors|Ionotropic Glutamate Receptors]] | + | *[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Frydenvang, K]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Kastrup, J S]] | + | [[Category: Frydenvang K]] |
| - | [[Category: Kristensen, L B]] | + | [[Category: Kastrup JS]] |
| - | [[Category: Kristensen, O]] | + | [[Category: Kristensen LB]] |
| - | [[Category: High-affinity kainate receptor]] | + | [[Category: Kristensen O]] |
| - | [[Category: Ion channel]]
| + | |
| - | [[Category: Ligand binding domain]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| 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 PubMed
Ionotropic 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 Also
References
- ↑ Kristensen O, Kristensen LB, Mollerud S, Frydenvang K, Pickering DS, Kastrup JS. The Structure of a High-Affinity Kainate Receptor: GluK4 Ligand-Binding Domain Crystallized with Kainate. Structure. 2016 Sep 6;24(9):1582-9. doi: 10.1016/j.str.2016.06.019. Epub 2016 Aug, 11. PMID:27524200 doi:http://dx.doi.org/10.1016/j.str.2016.06.019
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