Ontology highlight
ABSTRACT:
SUBMITTER: Branigan E
PROVIDER: S-EPMC4529489 | biostudies-literature | 2015 Aug
REPOSITORIES: biostudies-literature
Branigan Emma E Plechanovová Anna A Jaffray Ellis G EG Naismith James H JH Hay Ronald T RT
Nature structural & molecular biology 20150706 8
RING E3 ligase-catalyzed formation of K63-linked ubiquitin chains by the Ube2V2-Ubc13 E2 complex is required in many important biological processes. Here we report the structure of the RING-domain dimer of rat RNF4 in complex with a human Ubc13∼Ub conjugate and Ube2V2. The structure has captured Ube2V2 bound to the acceptor (priming) ubiquitin with K63 in a position favorable for attack on the linkage between Ubc13 and the donor (second) ubiquitin held in the active 'folded back' conformation by ...[more]