1b9y

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(New page: 200px<br /><applet load="1b9y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b9y, resolution 3.00&Aring;" /> '''STRUCTURAL ANALYSIS ...)
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[[Image:1b9y.gif|left|200px]]<br /><applet load="1b9y" size="350" color="white" frame="true" align="right" spinBox="true"
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'''STRUCTURAL ANALYSIS OF PHOSDUCIN AND ITS PHOSPHORYLATION-REGULATED INTERACTION WITH TRANSDUCIN BETA-GAMMA'''<br />
'''STRUCTURAL ANALYSIS OF PHOSDUCIN AND ITS PHOSPHORYLATION-REGULATED INTERACTION WITH TRANSDUCIN BETA-GAMMA'''<br />
==Overview==
==Overview==
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Visual signal transduction is a nearly noise-free process that is, exquisitely well regulated over a wide dynamic range of light intensity. A, key component in dark/light adaptation is phosducin, a phosphorylatable, protein that modulates the amount of transducin heterotrimer (Gt alpha, beta gamma) available through sequestration of the beta gamma subunits (Gt, beta gamma). The structure of the phosphophosducin/Gt beta gamma complex, combined with mutational and biophysical analysis provides a, stereochemical mechanism for the regulation of the phosducin-Gt beta gamma, interaction. Phosphorylation of serine 73 causes an order-to-disorder, transition of a 20-residue stretch, including the phosphorylation site, by, disrupting a helix-capping motif. This transition disrupts phosducin's, interface with Gt beta gamma, leading to the release of unencumbered Gt, beta gamma, which reassociates with the membrane and Gt alpha to form a, signaling-competent Gt alpha beta gamma heterotrimer.
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Visual signal transduction is a nearly noise-free process that is exquisitely well regulated over a wide dynamic range of light intensity. A key component in dark/light adaptation is phosducin, a phosphorylatable protein that modulates the amount of transducin heterotrimer (Gt alpha beta gamma) available through sequestration of the beta gamma subunits (Gt beta gamma). The structure of the phosphophosducin/Gt beta gamma complex combined with mutational and biophysical analysis provides a stereochemical mechanism for the regulation of the phosducin-Gt beta gamma interaction. Phosphorylation of serine 73 causes an order-to-disorder transition of a 20-residue stretch, including the phosphorylation site, by disrupting a helix-capping motif. This transition disrupts phosducin's interface with Gt beta gamma, leading to the release of unencumbered Gt beta gamma, which reassociates with the membrane and Gt alpha to form a signaling-competent Gt alpha beta gamma heterotrimer.
==About this Structure==
==About this Structure==
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1B9Y is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with GD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B9Y OCA].
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1B9Y is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=GD:'>GD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B9Y OCA].
==Reference==
==Reference==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Gaudet, R.]]
[[Category: Gaudet, R.]]
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[[Category: Sigler, P.B.]]
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[[Category: Sigler, P B.]]
[[Category: GD]]
[[Category: GD]]
[[Category: beta-gamma]]
[[Category: beta-gamma]]
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[[Category: vision]]
[[Category: vision]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:29:49 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:53:07 2008''

Revision as of 09:53, 21 February 2008


1b9y, resolution 3.00Å

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STRUCTURAL ANALYSIS OF PHOSDUCIN AND ITS PHOSPHORYLATION-REGULATED INTERACTION WITH TRANSDUCIN BETA-GAMMA

Overview

Visual signal transduction is a nearly noise-free process that is exquisitely well regulated over a wide dynamic range of light intensity. A key component in dark/light adaptation is phosducin, a phosphorylatable protein that modulates the amount of transducin heterotrimer (Gt alpha beta gamma) available through sequestration of the beta gamma subunits (Gt beta gamma). The structure of the phosphophosducin/Gt beta gamma complex combined with mutational and biophysical analysis provides a stereochemical mechanism for the regulation of the phosducin-Gt beta gamma interaction. Phosphorylation of serine 73 causes an order-to-disorder transition of a 20-residue stretch, including the phosphorylation site, by disrupting a helix-capping motif. This transition disrupts phosducin's interface with Gt beta gamma, leading to the release of unencumbered Gt beta gamma, which reassociates with the membrane and Gt alpha to form a signaling-competent Gt alpha beta gamma heterotrimer.

About this Structure

1B9Y is a Protein complex structure of sequences from Bos taurus and Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.

Reference

A molecular mechanism for the phosphorylation-dependent regulation of heterotrimeric G proteins by phosducin., Gaudet R, Savage JR, McLaughlin JN, Willardson BM, Sigler PB, Mol Cell. 1999 May;3(5):649-60. PMID:10360181

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