View source for 3qlv


==Crystal structure of the GluK2/GluK5 (GluR6/KA2) ATD tetramer assembly==
<StructureSection load='3qlv' size='340' side='right'caption='[[3qlv]], [[Resolution|resolution]] 3.94&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3qlv]] is a 10 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=3QLV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QLV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.94&#8491;</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=3qlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qlv OCA], [https://pdbe.org/3qlv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qlv RCSB], [https://www.ebi.ac.uk/pdbsum/3qlv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qlv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GRIK5_RAT GRIK5_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;">
== Publication Abstract from PubMed ==
Native glutamate receptor ion channels are tetrameric assemblies containing two or more different subunits. NMDA receptors are obligate heteromers formed by coassembly of two or three divergent gene families. While some AMPA and kainate receptors can form functional homomeric ion channels, the KA1 and KA2 subunits are obligate heteromers which function only in combination with GluR5-7. The mechanisms controlling glutamate receptor assembly involve an initial step in which the amino terminal domains (ATD) assemble as dimers. Here, we establish by sedimentation velocity that the ATDs of GluR6 and KA2 coassemble as a heterodimer of K(d) 11 nM, 32,000-fold lower than the K(d) for homodimer formation by KA2; we solve crystal structures for the GluR6/KA2 ATD heterodimer and heterotetramer assemblies. Using these structures as a guide, we perform a mutant cycle analysis to probe the energetics of assembly and show that high-affinity ATD interactions are required for biosynthesis of functional heteromeric receptors.

Structure and assembly mechanism for heteromeric kainate receptors.,Kumar J, Schuck P, Mayer ML Neuron. 2011 Jul 28;71(2):319-31. PMID:21791290<ref>PMID:21791290</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3qlv" style="background-color:#fffaf0;"></div>

==See Also==
*[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Kumar J]]
[[Category: Mayer ML]]