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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'''
| | ===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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17496150}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17496150 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17496150}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Pub domain]] | | [[Category: Pub domain]] |
| [[Category: Winged helix]] | | [[Category: Winged helix]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:33:08 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:27:25 2008'' |
