1mf6

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(New page: 200px<br /><applet load="1mf6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mf6" /> '''Transducin gamma subunit, C-terminal domain ...)
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[[Image:1mf6.jpg|left|200px]]<br /><applet load="1mf6" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mf6" />
 
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'''Transducin gamma subunit, C-terminal domain 60-71, rhodopsin-bound state: Ensemble of 15 models determined by TrNOE spectroscopy'''<br />
 
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==Overview==
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==Transducin gamma subunit, C-terminal domain 60-71, rhodopsin-bound state: Ensemble of 15 models determined by TrNOE spectroscopy==
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Rhodopsin, a prototypical G protein-coupled receptor, catalyzes the, activation of a heterotrimeric G protein, transducin, to initiate a visual, signaling cascade in photoreceptor cells. The betagamma subunit complex, especially the C-terminal domain of the transducin gamma subunit, Gtgamma(60-71)farnesyl, plays a pivotal role in allosteric regulation of, nucleotide exchange on the transducin alpha subunit by light-activated, rhodopsin. We report that this domain is unstructured in the presence of, an inactive receptor but forms an amphipathic helix upon rhodopsin, activation. A K65E/E66K charge reversal mutant of the gamma subunit has, diminished interactions with the receptor and fails to adopt the helical, conformation. The identification of this conformational switch provides a, mechanism for active GPCR utilization of the betagamma complex in signal, transfer to G proteins.
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<StructureSection load='1mf6' size='340' side='right'caption='[[1mf6]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1mf6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MF6 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1mf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mf6 OCA], [https://pdbe.org/1mf6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mf6 RCSB], [https://www.ebi.ac.uk/pdbsum/1mf6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mf6 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GBG1_BOVIN GBG1_BOVIN] 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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Rhodopsin, a prototypical G protein-coupled receptor, catalyzes the activation of a heterotrimeric G protein, transducin, to initiate a visual signaling cascade in photoreceptor cells. The betagamma subunit complex, especially the C-terminal domain of the transducin gamma subunit, Gtgamma(60-71)farnesyl, plays a pivotal role in allosteric regulation of nucleotide exchange on the transducin alpha subunit by light-activated rhodopsin. We report that this domain is unstructured in the presence of an inactive receptor but forms an amphipathic helix upon rhodopsin activation. A K65E/E66K charge reversal mutant of the gamma subunit has diminished interactions with the receptor and fails to adopt the helical conformation. The identification of this conformational switch provides a mechanism for active GPCR utilization of the betagamma complex in signal transfer to G proteins.
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==About this Structure==
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Rhodopsin controls a conformational switch on the transducin gamma subunit.,Kisselev OG, Downs MA Structure. 2003 Apr;11(4):367-73. PMID:12679015<ref>PMID:12679015</ref>
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1MF6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MF6 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Rhodopsin controls a conformational switch on the transducin gamma subunit., Kisselev OG, Downs MA, Structure. 2003 Apr;11(4):367-73. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12679015 12679015]
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</div>
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<div class="pdbe-citations 1mf6" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Kisselev, O.G.]]
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[[Category: Kisselev OG]]
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[[Category: bound conformation]]
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[[Category: c-terminal domain]]
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[[Category: g-protein]]
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[[Category: gamma subunit]]
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[[Category: gpcr]]
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[[Category: rhodopsin]]
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[[Category: transducin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:22:59 2007''
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Current revision

Transducin gamma subunit, C-terminal domain 60-71, rhodopsin-bound state: Ensemble of 15 models determined by TrNOE spectroscopy

PDB ID 1mf6

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