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==Crystal structure of a human GABAB receptor peptide bound to KCTD16 T1==
<StructureSection load='6ocp' size='340' side='right'caption='[[6ocp]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ocp]] is a 18 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=6OCP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OCP 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]] 2.35&#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=6ocp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ocp OCA], [https://pdbe.org/6ocp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ocp RCSB], [https://www.ebi.ac.uk/pdbsum/6ocp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ocp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KCD16_HUMAN KCD16_HUMAN] Auxiliary subunit of GABA-B receptors that determine the pharmacology and kinetics of the receptor response. Increases agonist potency and markedly alter the G-protein signaling of the receptors by accelerating onset and promoting desensitization (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Metabotropic GABAB receptors mediate a significant fraction of inhibitory neurotransmission in the brain. Native GABAB receptor complexes contain the principal subunits GABAB1 and GABAB2, which form an obligate heterodimer, and auxiliary subunits, known as potassium channel tetramerization domain-containing proteins (KCTDs). KCTDs interact with GABAB receptors and modify the kinetics of GABAB receptor signaling. Little is known about the molecular mechanism governing the direct association and functional coupling of GABAB receptors with these auxiliary proteins. Here, we describe the high-resolution structure of the KCTD16 oligomerization domain in complex with part of the GABAB2 receptor. A single GABAB2 C-terminal peptide is bound to the interior of an open pentamer formed by the oligomerization domain of five KCTD16 subunits. Mutation of specific amino acids identified in the structure of the GABAB2-KCTD16 interface disrupted both the biochemical association and functional modulation of GABAB receptors and G protein-activated inwardly rectifying K(+) channel (GIRK) channels. These interfacial residues are conserved among KCTDs, suggesting a common mode of KCTD interaction with GABAB receptors. Defining the binding interface of GABAB receptor and KCTD reveals a potential regulatory site for modulating GABAB-receptor function in the brain.

Structural basis for auxiliary subunit KCTD16 regulation of the GABAB receptor.,Zuo H, Glaaser I, Zhao Y, Kurinov I, Mosyak L, Wang H, Liu J, Park J, Frangaj A, Sturchler E, Zhou M, McDonald P, Geng Y, Slesinger PA, Fan QR Proc Natl Acad Sci U S A. 2019 Apr 10. pii: 1903024116. doi:, 10.1073/pnas.1903024116. PMID:30971491<ref>PMID:30971491</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ocp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Fan QR]]
[[Category: Frangaj A]]
[[Category: Geng Y]]
[[Category: Glaaser I]]
[[Category: Kurinov I]]
[[Category: Liu J]]
[[Category: McDonald P]]
[[Category: Mosyak L]]
[[Category: Park J]]
[[Category: Slesinger PA]]
[[Category: Sturchler E]]
[[Category: Wang H]]
[[Category: Zhao Y]]
[[Category: Zhou M]]
[[Category: Zuo H]]