Ontology highlight
ABSTRACT:
SUBMITTER: Dove KK
PROVIDER: S-EPMC4967960 | biostudies-literature | 2016 Aug
REPOSITORIES: biostudies-literature
Dove Katja K KK Stieglitz Benjamin B Duncan Emily D ED Rittinger Katrin K Klevit Rachel E RE
EMBO reports 20160616 8
RING-in-between-RING (RBR) ubiquitin (Ub) ligases are a distinct class of E3s, defined by a RING1 domain that binds E2 Ub-conjugating enzyme and a RING2 domain that contains an active site cysteine similar to HECT-type E3s. Proposed to function as RING/HECT hybrids, details regarding the Ub transfer mechanism used by RBRs have yet to be defined. When paired with RING-type E3s, E2s perform the final step of Ub ligation to a substrate. In contrast, when paired with RBR E3s, E2s must transfer Ub on ...[more]