Ontology highlight
ABSTRACT:
SUBMITTER: Bebeacua C
PROVIDER: S-EPMC3268311 | biostudies-literature | 2012 Jan
REPOSITORIES: biostudies-literature
Bebeacua Cecilia C Förster Andreas A McKeown Ciarán C Meyer Hemmo H HH Zhang Xiaodong X Freemont Paul S PS
Proceedings of the National Academy of Sciences of the United States of America 20120109 4
p97 is a key regulator of numerous cellular pathways and associates with ubiquitin-binding adaptors to remodel ubiquitin-modified substrate proteins. How adaptor binding to p97 is coordinated and how adaptors contribute to substrate remodeling is unclear. Here we present the 3D electron cryomicroscopy reconstructions of the major Ufd1-Npl4 adaptor in complex with p97. Our reconstructions show that p97-Ufd1-Npl4 is highly dynamic and that Ufd1-Npl4 assumes distinct positions relative to the p97 r ...[more]