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2pbi

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==The multifunctional nature of Gbeta5/RGS9 revealed from its crystal structure==
==The multifunctional nature of Gbeta5/RGS9 revealed from its crystal structure==
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<StructureSection load='2pbi' size='340' side='right' caption='[[2pbi]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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<StructureSection load='2pbi' size='340' side='right'caption='[[2pbi]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2pbi]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PBI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PBI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2pbi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PBI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PBI FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rgs9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), Gnb5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<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=2pbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pbi OCA], [http://pdbe.org/2pbi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pbi RCSB], [http://www.ebi.ac.uk/pdbsum/2pbi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2pbi ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pbi OCA], [https://pdbe.org/2pbi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pbi RCSB], [https://www.ebi.ac.uk/pdbsum/2pbi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pbi ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/RGS9_MOUSE RGS9_MOUSE]] Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G(t)-alpha. Involved in phototransduction; key element in the recovery phase of visual transduction. [[http://www.uniprot.org/uniprot/GBB5_MOUSE GBB5_MOUSE]] 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.
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[https://www.uniprot.org/uniprot/RGS9_MOUSE RGS9_MOUSE] Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G(t)-alpha. Involved in phototransduction; key element in the recovery phase of visual transduction.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pb/2pbi_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pb/2pbi_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2pbi ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2pbi ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Regulators of G-protein signaling (RGS) proteins enhance the intrinsic GTPase activity of G protein alpha (Galpha) subunits and are vital for proper signaling kinetics downstream of G protein-coupled receptors (GPCRs). R7 subfamily RGS proteins specifically and obligately dimerize with the atypical G protein beta5 (Gbeta5) subunit through an internal G protein gamma (Ggamma)-subunit-like (GGL) domain. Here we present the 1.95-A crystal structure of the Gbeta5-RGS9 complex, which is essential for normal visual and neuronal signal transduction. This structure reveals a canonical RGS domain that is functionally integrated within a molecular complex that is poised for integration of multiple steps during G-protein activation and deactivation.
 
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Crystal structure of the multifunctional Gbeta5-RGS9 complex.,Cheever ML, Snyder JT, Gershburg S, Siderovski DP, Harden TK, Sondek J Nat Struct Mol Biol. 2008 Feb;15(2):155-62. Epub 2008 Jan 20. PMID:18204463<ref>PMID:18204463</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 2pbi" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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*[[Regulator of G protein signaling|Regulator of G protein signaling]]
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*[[Regulator of G-protein signaling 3D structures|Regulator of G-protein signaling 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Lk3 transgenic mice]]
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[[Category: Large Structures]]
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[[Category: Cheever, M L]]
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[[Category: Mus musculus]]
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[[Category: Gershburg, S]]
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[[Category: Cheever ML]]
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[[Category: Harden, T K]]
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[[Category: Gershburg S]]
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[[Category: Siderovski, D P]]
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[[Category: Harden TK]]
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[[Category: Snyder, J T]]
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[[Category: Siderovski DP]]
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[[Category: Sondek, J]]
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[[Category: Snyder JT]]
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[[Category: Beta propeller]]
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[[Category: Sondek J]]
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[[Category: Dep domain]]
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[[Category: Dhex domain]]
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[[Category: Ggl domain]]
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[[Category: Helix wrap]]
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[[Category: Rgs domain]]
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[[Category: Signaling protein]]
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The multifunctional nature of Gbeta5/RGS9 revealed from its crystal structure

PDB ID 2pbi

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