1b9y

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{{Seed}}
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{{STRUCTURE_1b9y| PDB=1b9y | SCENE= }}
{{STRUCTURE_1b9y| PDB=1b9y | SCENE= }}
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'''STRUCTURAL ANALYSIS OF PHOSDUCIN AND ITS PHOSPHORYLATION-REGULATED INTERACTION WITH TRANSDUCIN BETA-GAMMA'''
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===STRUCTURAL ANALYSIS OF PHOSDUCIN AND ITS PHOSPHORYLATION-REGULATED INTERACTION WITH TRANSDUCIN BETA-GAMMA===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 10360181 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10360181}}
==About this Structure==
==About this Structure==
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[[Category: Transducin]]
[[Category: Transducin]]
[[Category: Vision]]
[[Category: Vision]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:15:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:39:48 2008''

Revision as of 15:39, 30 June 2008

Image:1b9y.png

Template:STRUCTURE 1b9y

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

Template:ABSTRACT PUBMED 10360181

About this Structure

1B9Y is a Protein complex structure of sequences from Bos taurus and Rattus norvegicus. 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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