2bt2: Difference between revisions

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[[Image:2bt2.png|left|200px]]
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{{STRUCTURE_2bt2|  PDB=2bt2  |  SCENE=  }}  
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===STRUCTURE OF THE REGULATOR OF G-PROTEIN SIGNALING 16===
===STRUCTURE OF THE REGULATOR OF G-PROTEIN SIGNALING 16===
{{ABSTRACT_PUBMED_18434541}}


 
==Function==
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[[http://www.uniprot.org/uniprot/RGS16_HUMAN RGS16_HUMAN]] Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G(i)-alpha and G(o)-alpha, but not to G(s)-alpha. May play a role in regulating the kinetics of signaling in the phototransduction cascade.  
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{{ABSTRACT_PUBMED_18434541}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
<ref group="xtra">PMID:018434541</ref><references group="xtra"/>
<ref group="xtra">PMID:018434541</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Arrowsmith, C.]]
[[Category: Arrowsmith, C.]]

Revision as of 11:34, 23 April 2014

Template:STRUCTURE 2bt2

STRUCTURE OF THE REGULATOR OF G-PROTEIN SIGNALING 16STRUCTURE OF THE REGULATOR OF G-PROTEIN SIGNALING 16

Template:ABSTRACT PUBMED 18434541

FunctionFunction

[RGS16_HUMAN] Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G(i)-alpha and G(o)-alpha, but not to G(s)-alpha. May play a role in regulating the kinetics of signaling in the phototransduction cascade.

About this StructureAbout this Structure

2bt2 is a 5 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. Soundararajan M, Willard FS, Kimple AJ, Turnbull AP, Ball LJ, Schoch GA, Gileadi C, Fedorov OY, Dowler EF, Higman VA, Hutsell SQ, Sundstrom M, Doyle DA, Siderovski DP. Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits. Proc Natl Acad Sci U S A. 2008 Apr 29;105(17):6457-62. Epub 2008 Apr 23. PMID:18434541

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OCA