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1mf6
From Proteopedia
(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=" | + | [[Image:1mf6.jpg|left|200px]]<br /><applet load="1mf6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mf6" /> | caption="1mf6" /> | ||
'''Transducin gamma subunit, C-terminal domain 60-71, rhodopsin-bound state: Ensemble of 15 models determined by TrNOE spectroscopy'''<br /> | '''Transducin gamma subunit, C-terminal domain 60-71, rhodopsin-bound state: Ensemble of 15 models determined by TrNOE spectroscopy'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Rhodopsin, a prototypical G protein-coupled receptor, catalyzes the | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 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:// | + | 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1MF6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Kisselev, O | + | [[Category: Kisselev, O G.]] |
[[Category: bound conformation]] | [[Category: bound conformation]] | ||
[[Category: c-terminal domain]] | [[Category: c-terminal domain]] | ||
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[[Category: transducin]] | [[Category: transducin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:54:49 2008'' |
Revision as of 11:54, 21 February 2008
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Transducin gamma subunit, C-terminal domain 60-71, rhodopsin-bound state: Ensemble of 15 models determined by TrNOE spectroscopy
Overview
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.
About this Structure
1MF6 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Rhodopsin controls a conformational switch on the transducin gamma subunit., Kisselev OG, Downs MA, Structure. 2003 Apr;11(4):367-73. PMID:12679015
Page seeded by OCA on Thu Feb 21 13:54:49 2008
