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2ccq
From Proteopedia
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| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:49:59 2007'' |
Revision as of 08:45, 30 October 2007
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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, ... [(full description)]
About this Structure
2CCQ is a [Single protein] structure of sequence from [Homo sapiens] with GOL as [ligand]. Structure known Active Site: AC1. 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
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