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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]] 2.05&Aring;' scene=''>
<StructureSection load='5ikb' size='340' side='right'caption='[[5ikb]], [[Resolution|resolution]] 2.05&Aring;' 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 [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]] 2.05&#8491;</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='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'>[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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</div>
</div>
<div class="pdbe-citations 5ikb" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5ikb" style="background-color:#fffaf0;"></div>
==See Also==
*[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Frydenvang, K]]
[[Category: Large Structures]]
[[Category: Kastrup, J S]]
[[Category: Rattus norvegicus]]
[[Category: Kristensen, L B]]
[[Category: Frydenvang K]]
[[Category: Kristensen, O]]
[[Category: Kastrup JS]]
[[Category: High-affinity kainate receptor]]
[[Category: Kristensen LB]]
[[Category: Ion channel]]
[[Category: Kristensen O]]
[[Category: Ligand binding domain]]
[[Category: Membrane protein]]

Latest revision as of 16:58, 30 August 2023

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

5ikb is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.05Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

  1. 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

5ikb, resolution 2.05Å

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