2r2y: Difference between revisions
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{{STRUCTURE_2r2y| PDB=2r2y | SCENE= }} | {{STRUCTURE_2r2y| PDB=2r2y | SCENE= }} | ||
===Crystal structure of the proteasomal Rpn13 PRU-domain=== | ===Crystal structure of the proteasomal Rpn13 PRU-domain=== | ||
{{ABSTRACT_PUBMED_18497827}} | |||
==Function== | |||
[[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== | ||
<ref group="xtra">PMID:018497827</ref><references group="xtra"/> | <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
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
- ↑ 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
- ↑ 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
