2hpj
From Proteopedia
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[[Image:2hpj.jpg|left|200px]] | [[Image:2hpj.jpg|left|200px]] | ||
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'''Crystal structure of the PUB domain of mouse PNGase''' | '''Crystal structure of the PUB domain of mouse PNGase''' | ||
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17496150 17496150] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17496150 17496150] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | [[Category: Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Lennarz, W.]] | [[Category: Lennarz, W.]] | ||
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[[Category: Zhao, G.]] | [[Category: Zhao, G.]] | ||
[[Category: Zhou, X.]] | [[Category: Zhou, X.]] | ||
| - | [[Category: | + | [[Category: Pub domain]] |
| - | [[Category: | + | [[Category: Winged helix]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:33:05 2008'' | |
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Revision as of 03:33, 4 May 2008
Crystal structure of the PUB domain of mouse PNGase
Overview
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.
About this Structure
2HPJ 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 Page seeded by OCA on Sun May 4 06:33:05 2008
Categories: Mus musculus | Single protein | Lennarz, W. | Li, G. | Schindelin, H. | Wang, L. | Zhao, G. | Zhou, X. | Pub domain | Winged helix
