2cm0: Difference between revisions

Revision as of 17:50, 21 February 2008

THE PUB DOMAIN FUNCTIONS AS A P97 BINDING MODULE IN HUMAN PEPTIDE N-GLYCANASE.

OverviewOverview

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 StructureAbout this Structure

2CM0 is a Single protein structure of sequence from Homo sapiens with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

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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 ==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.
+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==
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 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Allen, M.D.]]
+[[Category: Allen, M D.]]
 [[Category: Buchberger, A.]]
 [[Category: Bycroft, M.]]
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 [[Category: transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:36:46 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:50:03 2008''