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'''THE PUB DOMAIN FUNCTIONS AS A P97 BINDING MODULE IN HUMAN PEPTIDE N-GLYCANASE.''' | '''THE PUB DOMAIN FUNCTIONS AS A P97 BINDING MODULE IN HUMAN PEPTIDE N-GLYCANASE.''' | ||
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[[Category: Buchberger, A.]] | [[Category: Buchberger, A.]] | ||
[[Category: Bycroft, M.]] | [[Category: Bycroft, M.]] | ||
[[Category: | [[Category: Kinase]] | ||
[[Category: | [[Category: Pug domain]] | ||
[[Category: | [[Category: Transferase]] | ||
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Revision as of 19:28, 3 May 2008
THE PUB DOMAIN FUNCTIONS AS A P97 BINDING MODULE IN HUMAN PEPTIDE N-GLYCANASE.
Overview
The AAA ATPase p97 is a ubiquitin-selective molecular machine involved in multiple cellular processes, including protein degradation through the ubiquitin-proteasome system and homotypic membrane fusion. Specific p97 functions are mediated by a variety of cofactors, among them peptide N-glycanase, an enzyme that removes glycans from misfolded glycoproteins. Here we report the three-dimensional structure of the aminoterminal PUB domain of human peptide N-glycanase. We demonstrate that the PUB domain is a novel p97 binding module interacting with the D1 and/or D2 ATPase domains of p97 and identify an evolutionary conserved surface patch required for p97 binding. Furthermore, we show that the PUB and UBX domains do not bind to p97 in a mutually exclusive manner. Our results suggest that PUB domain-containing proteins constitute a widespread family of diverse p97 cofactors.
About this Structure
2CM0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The PUB domain functions as a p97 binding module in human peptide N-glycanase., Allen MD, Buchberger A, Bycroft M, J Biol Chem. 2006 Sep 1;281(35):25502-8. Epub 2006 Jun 28. PMID:16807242 Page seeded by OCA on Sat May 3 22:28:10 2008
