1b9y: Difference between revisions

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[[Image:1b9y.gif|left|200px]]
{{Seed}}
[[Image:1b9y.png|left|200px]]


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{{STRUCTURE_1b9y|  PDB=1b9y  |  SCENE=  }}  
{{STRUCTURE_1b9y|  PDB=1b9y  |  SCENE=  }}  


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




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_10360181}}, adds the Publication Abstract to the page
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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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