6m8s: Difference between revisions

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~~'''Unreleased structure'''~~

The ~~entry 6m8s~~ is ~~ON HOLD~~

==Crystal structure of the KCTD12 H1 domain in complex with Gbeta1gamma2 subunits==

== Structural highlights ==

<table><tr><td colspan='2'>[[6m8s]] is a 15 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=6M8S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M8S 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]] 3.71Å</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=6m8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m8s OCA], [https://pdbe.org/6m8s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m8s RCSB], [https://www.ebi.ac.uk/pdbsum/6m8s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m8s ProSAT]</span></td></tr>

</table>

== Function ==

[https://www.uniprot.org/uniprot/GBB1_HUMAN GBB1_HUMAN] Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.<ref>PMID:18611381</ref>

== Publication Abstract from PubMed ==

The GABAB (gamma-aminobutyric acid type B) receptor is one of the principal inhibitory neurotransmitter receptors in the brain, and it signals through heterotrimeric G proteins to activate a variety of effectors, including G-protein-coupled inwardly rectifying potassium channels (GIRKs)(1,2). GABAB-receptor signalling is tightly regulated by auxiliary subunits called KCTDs, which control the kinetics of GIRK activation and desensitization(3-5). However, the mechanistic basis for KCTD modulation of GABAB signalling remains incompletely understood. Here, using a combination of X-ray crystallography, electron microscopy, and functional and biochemical experiments, we reveal the molecular details of KCTD binding to both GABAB receptors and G-protein betagamma subunits. KCTDs associate with the receptor by forming an asymmetric pentameric ring around a region of the receptor carboxy-terminal tail, while a second KCTD domain, H1, engages in a symmetric interaction with five copies of Gbetagamma in which the G-protein subunits also interact directly with one another. We further show that KCTD binding to Gbetagamma is highly cooperative, defining a model in which KCTD proteins cooperatively strip G proteins from GIRK channels to induce rapid desensitization following receptor activation. These results provide a framework for understanding the molecular basis for the precise temporal control of GABAB signalling by KCTD proteins.

~~Authors~~:

Structural basis for KCTD-mediated rapid desensitization of GABAB signalling.,Zheng S, Abreu N, Levitz J, Kruse AC Nature. 2019 Mar;567(7746):127-131. doi: 10.1038/s41586-019-0990-0. Epub 2019 Feb, 27. PMID:30814734<ref>PMID:30814734</ref>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

==See Also==

*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]]

*[[Transducin 3D structures|Transducin 3D structures]]

== References ==

__TOC__

</StructureSection>

[[Category: Homo sapiens]]

[[Category: Large Structures]]

[[Category: Kruse AC]]

[[Category: Zheng S]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6m8s is ON HOLD
+==Crystal structure of the KCTD12 H1 domain in complex with Gbeta1gamma2 subunits==
+<StructureSection load='6m8s' size='340' side='right'caption='[[6m8s]], [[Resolution|resolution]] 3.71&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6m8s]] is a 15 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=6M8S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M8S 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]] 3.71&#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=6m8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m8s OCA], [https://pdbe.org/6m8s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m8s RCSB], [https://www.ebi.ac.uk/pdbsum/6m8s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m8s ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/GBB1_HUMAN GBB1_HUMAN] Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.<ref>PMID:18611381</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The GABAB (gamma-aminobutyric acid type B) receptor is one of the principal inhibitory neurotransmitter receptors in the brain, and it signals through heterotrimeric G proteins to activate a variety of effectors, including G-protein-coupled inwardly rectifying potassium channels (GIRKs)(1,2). GABAB-receptor signalling is tightly regulated by auxiliary subunits called KCTDs, which control the kinetics of GIRK activation and desensitization(3-5). However, the mechanistic basis for KCTD modulation of GABAB signalling remains incompletely understood. Here, using a combination of X-ray crystallography, electron microscopy, and functional and biochemical experiments, we reveal the molecular details of KCTD binding to both GABAB receptors and G-protein betagamma subunits. KCTDs associate with the receptor by forming an asymmetric pentameric ring around a region of the receptor carboxy-terminal tail, while a second KCTD domain, H1, engages in a symmetric interaction with five copies of Gbetagamma in which the G-protein subunits also interact directly with one another. We further show that KCTD binding to Gbetagamma is highly cooperative, defining a model in which KCTD proteins cooperatively strip G proteins from GIRK channels to induce rapid desensitization following receptor activation. These results provide a framework for understanding the molecular basis for the precise temporal control of GABAB signalling by KCTD proteins.
-Authors:
+Structural basis for KCTD-mediated rapid desensitization of GABAB signalling.,Zheng S, Abreu N, Levitz J, Kruse AC Nature. 2019 Mar;567(7746):127-131. doi: 10.1038/s41586-019-0990-0. Epub 2019 Feb, 27. PMID:30814734<ref>PMID:30814734</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6m8s" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]]
+*[[Transducin 3D structures|Transducin 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Kruse AC]]
+[[Category: Zheng S]]