View source for 4f11


==Crystal structure of the extracellular domain of human GABA(B) receptor GBR2==
<StructureSection load='4f11' size='340' side='right'caption='[[4f11]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4f11]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F11 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F11 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]] 2.38&#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=4f11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f11 OCA], [https://pdbe.org/4f11 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f11 RCSB], [https://www.ebi.ac.uk/pdbsum/4f11 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f11 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Inhibitory neurotransmission is mediated primarily by GABA. The metabotropic GABA(B) receptor is a G protein-coupled receptor central to mammalian brain function. Malfunction of GABA(B) receptor has been implicated in several neurological disorders. GABA(B) receptor functions as a heterodimeric assembly of GBR1 and GBR2 subunits, where GBR1 is responsible for ligand-binding and GBR2 is responsible for G protein coupling. Here we demonstrate that the GBR2 ectodomain directly interacts with the GBR1 ectodomain to increase agonist affinity by selectively stabilizing the agonist-bound conformation of GBR1. We present the crystal structure of the GBR2 ectodomain, which reveals a polar heterodimeric interface. We also identify specific heterodimer contacts from both subunits, and GBR1 residues involved in ligand recognition. Lastly, our structural and functional data indicate that the GBR2 ectodomain adopts a constitutively open conformation, suggesting a structural asymmetry in the active state of GABA(B) receptor that is unique to the GABAergic system.

Structure and functional interaction of the extracellular domain of human GABA(B) receptor GBR2.,Geng Y, Xiong D, Mosyak L, Malito DL, Kniazeff J, Chen Y, Burmakina S, Quick M, Bush M, Javitch JA, Pin JP, Fan QR Nat Neurosci. 2012 Jun 3;15(7):970-8. doi: 10.1038/nn.3133. PMID:22660477<ref>PMID:22660477</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4f11" style="background-color:#fffaf0;"></div>

==See Also==
*[[GABA receptor 3D structures|GABA receptor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Burmakina S]]
[[Category: Bush M]]
[[Category: Chen Y]]
[[Category: Fan QR]]
[[Category: Geng Y]]
[[Category: Javitch JA]]
[[Category: Kniazeff J]]
[[Category: Malito DL]]
[[Category: Mosyak L]]
[[Category: Pin J-P]]
[[Category: Quick M]]
[[Category: Xiong D]]