3psp

From Proteopedia

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m (Protected "3psp" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_3psp| PDB=3psp | SCENE= }}
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===Crystal structure of PUL and PFU domain===
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The entry 3psp is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/DOA1_YEAST DOA1_YEAST]] Participates in the regulation of the ubiquitin conjugation pathway involving CDC48 by hindering multiubiquitination of substrates at the CDC48 chaperone. May act by preventing the interaction between CDC48 and the E4 enzyme UFD2, leading to prevent multiubiquitination of substrates and subsequent degradation. Essential for maintaining cellular ubiquitin levels.<ref>PMID:15096053</ref> <ref>PMID:8890162</ref>
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Authors: Liu, Y., Sun, J.
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==About this Structure==
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[[3psp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PSP OCA].
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Description: Crystal structure of PUL and PFU domain
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==Reference==
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<references group="xtra"/><references/>
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Liu, Y.]]
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[[Category: Sun, J.]]
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[[Category: Cdc48 ubiquitin]]
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[[Category: Maintain the ubiquitin level]]
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[[Category: Nuclear protein]]
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[[Category: Protein degradation]]

Revision as of 08:06, 8 May 2013

Template:STRUCTURE 3psp

Contents

Crystal structure of PUL and PFU domain

Function

[DOA1_YEAST] Participates in the regulation of the ubiquitin conjugation pathway involving CDC48 by hindering multiubiquitination of substrates at the CDC48 chaperone. May act by preventing the interaction between CDC48 and the E4 enzyme UFD2, leading to prevent multiubiquitination of substrates and subsequent degradation. Essential for maintaining cellular ubiquitin levels.[1] [2]

About this Structure

3psp is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

  1. ↑ Russell NS, Wilkinson KD. Identification of a novel 29-linked polyubiquitin binding protein, Ufd3, using polyubiquitin chain analogues. Biochemistry. 2004 Apr 27;43(16):4844-54. PMID:15096053 doi:10.1021/bi035626r
  2. ↑ Ghislain M, Dohmen RJ, Levy F, Varshavsky A. Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae. EMBO J. 1996 Sep 16;15(18):4884-99. PMID:8890162

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OCA

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