Ontology highlight
ABSTRACT:
SUBMITTER: Dove KK
PROVIDER: S-EPMC5462532 | biostudies-literature | 2017 Jun
REPOSITORIES: biostudies-literature
Dove Katja K KK Olszewski Jennifer L JL Martino Luigi L Duda David M DM Wu Xiaoli S XS Miller Darcie J DJ Reiter Katherine H KH Rittinger Katrin K Schulman Brenda A BA Klevit Rachel E RE
Structure (London, England : 1993) 20170525 6
RING-between-RING (RBR) E3s contain RING1 domains that are structurally similar yet mechanistically distinct from canonical RING domains. Both types of E3 bind E2∼ubiquitin (E2∼Ub) via their RINGs but canonical RING E3s promote closed E2∼Ub conformations required for direct Ub transfer from the E2 to substrate, while RBR RING1s promote open E2∼Ub to favor Ub transfer to the E3 active site. This different RING/E2∼Ub conformation determines its direct target, which for canonical RING E3s is typica ...[more]