2ccq

Publication Abstract from PubMed

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 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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.