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="350" color="white" frame="true" align="right" spinBox="true"
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'''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==
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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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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==
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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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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]]
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[[Category: Kisselev, O.G.]]
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[[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]]
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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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''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


1mf6

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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

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