3ugx

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[[Image:3ugx.png|left|200px]]
 
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{{STRUCTURE_3ugx| PDB=3ugx | SCENE= }}
{{STRUCTURE_3ugx| PDB=3ugx | SCENE= }}
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===Crystal Structure of Visual Arrestin===
===Crystal Structure of Visual Arrestin===
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{{ABSTRACT_PUBMED_22306737}}
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==Disease==
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[[http://www.uniprot.org/uniprot/ARRS_BOVIN ARRS_BOVIN]] Note=S-antigen induces autoimmune uveitis.
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==Function==
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[[http://www.uniprot.org/uniprot/ARRS_BOVIN ARRS_BOVIN]] Arrestin is one of the major proteins of the ros (retinal rod outer segments); it binds to photoactivated-phosphorylated rhodopsin, thereby apparently preventing the transducin-mediated activation of phosphodiesterase. Isoform B plays a role in the phototransduction cascade.
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(as it appears on PubMed at http://www.pubmed.gov), where 22306737 is the PubMed ID number.
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{{ABSTRACT_PUBMED_22306737}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:022306737</ref><references group="xtra"/>
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<ref group="xtra">PMID:022306737</ref><references group="xtra"/><references/>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Batra-Safferling, R.]]
[[Category: Batra-Safferling, R.]]

Revision as of 16:47, 24 March 2013

Template:STRUCTURE 3ugx

Contents

Crystal Structure of Visual Arrestin

Template:ABSTRACT PUBMED 22306737

Disease

[ARRS_BOVIN] Note=S-antigen induces autoimmune uveitis.

Function

[ARRS_BOVIN] Arrestin is one of the major proteins of the ros (retinal rod outer segments); it binds to photoactivated-phosphorylated rhodopsin, thereby apparently preventing the transducin-mediated activation of phosphodiesterase. Isoform B plays a role in the phototransduction cascade.

About this Structure

3ugx is a 4 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

  • Granzin J, Cousin A, Weirauch M, Schlesinger R, Buldt G, Batra-Safferling R. Crystal Structure of p44, a Constitutively Active Splice Variant of Visual Arrestin. J Mol Biol. 2012 Mar 9;416(5):611-8. Epub 2012 Jan 27. PMID:22306737 doi:10.1016/j.jmb.2012.01.028

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OCA

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