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2r2y

From Proteopedia

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[[Image:2r2y.png|left|200px]]
 
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{{STRUCTURE_2r2y| PDB=2r2y | SCENE= }}
{{STRUCTURE_2r2y| PDB=2r2y | SCENE= }}
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===Crystal structure of the proteasomal Rpn13 PRU-domain===
===Crystal structure of the proteasomal Rpn13 PRU-domain===
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{{ABSTRACT_PUBMED_18497827}}
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{{ABSTRACT_PUBMED_18497827}}
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==Function==
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[[http://www.uniprot.org/uniprot/ADRM1_MOUSE ADRM1_MOUSE]] Functions as a proteasomal ubiquitin receptor. Recruits the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity.<ref>PMID:15819879</ref> <ref>PMID:18497827</ref>
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:018497827</ref><references group="xtra"/>
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<ref group="xtra">PMID:018497827</ref><references group="xtra"/><references/>
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Dikic, I.]]
[[Category: Dikic, I.]]

Revision as of 08:03, 30 June 2013

Template:STRUCTURE 2r2y

Contents

Crystal structure of the proteasomal Rpn13 PRU-domain

Template:ABSTRACT PUBMED 18497827

Function

[ADRM1_MOUSE] Functions as a proteasomal ubiquitin receptor. Recruits the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity.[1] [2]

About this Structure

2r2y is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

  • Schreiner P, Chen X, Husnjak K, Randles L, Zhang N, Elsasser S, Finley D, Dikic I, Walters KJ, Groll M. Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction. Nature. 2008 May 22;453(7194):548-52. PMID:18497827 doi:10.1038/nature06924
  1. ↑ Lamerant N, Kieda C. Adhesion properties of adhesion-regulating molecule 1 protein on endothelial cells. FEBS J. 2005 Apr;272(8):1833-44. PMID:15819879 doi:10.1111/j.1742-4658.2005.04613.x
  2. ↑ Schreiner P, Chen X, Husnjak K, Randles L, Zhang N, Elsasser S, Finley D, Dikic I, Walters KJ, Groll M. Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction. Nature. 2008 May 22;453(7194):548-52. PMID:18497827 doi:10.1038/nature06924

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OCA

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