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2hpl

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{{STRUCTURE_2hpl| PDB=2hpl | SCENE= }}
{{STRUCTURE_2hpl| PDB=2hpl | SCENE= }}
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'''Crystal structure of the mouse p97/PNGase complex'''
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===Crystal structure of the mouse p97/PNGase complex===
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==Overview==
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During endoplasmic reticulum-associated degradation, the multifunctional AAA ATPase p97 is part of a protein degradation complex. p97 associates via its N-terminal domain with various cofactors to recruit ubiquitinated substrates. It also interacts with alternative substrate-processing cofactors, such as Ufd2, Ufd3, and peptide:N-glycanase (PNGase) in higher eukaryotes. These cofactors determine different fates of the substrates and they all bind outside of the N-terminal domain of p97. Here, we describe a cofactor-binding motif of p97 contained within the last 10 amino acid residues of the C terminus, which is both necessary and sufficient to mediate interactions of p97 with PNGase and Ufd3. The crystal structure of the N-terminal domain of PNGase in complex with this motif provides detailed insight into the interaction between p97 and its substrate-processing cofactors. Phosphorylation of p97's highly conserved penultimate tyrosine residue, which is the main phosphorylation site during T cell receptor stimulation, completely blocks binding of either PNGase or Ufd3 to p97. This observation suggests that phosphorylation of this residue modulates endoplasmic reticulum-associated protein degradation activity by discharging substrate-processing cofactors.
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(as it appears on PubMed at http://www.pubmed.gov), where 17496150 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17496150}}
==About this Structure==
==About this Structure==
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:33:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:27:25 2008''

Revision as of 09:27, 28 July 2008

Image:2hpl.png

Template:STRUCTURE 2hpl

Crystal structure of the mouse p97/PNGase complex

Template:ABSTRACT PUBMED 17496150

About this Structure

2HPL is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Studies on peptide:N-glycanase-p97 interaction suggest that p97 phosphorylation modulates endoplasmic reticulum-associated degradation., Zhao G, Zhou X, Wang L, Li G, Schindelin H, Lennarz WJ, Proc Natl Acad Sci U S A. 2007 May 22;104(21):8785-90. Epub 2007 May 11. PMID:17496150

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