Ontology highlight
ABSTRACT:
SUBMITTER: Yagi H
PROVIDER: S-EPMC3343348 | biostudies-literature | 2012 May
REPOSITORIES: biostudies-literature
EMBO reports 20120501 5
HOIL-1L and its binding partner HOIP are essential components of the E3-ligase complex that generates linear ubiquitin (Ub) chains, which are critical regulators of NF-κB activation. Using crystallographic and mutational approaches, we characterize the unexpected structural basis for the specific interaction between the Ub-like domain (UBL) of HOIL-1L and the Ub-associated domain (UBA) of HOIP. Our data indicate the functional significance of this non-canonical mode of UBA-UBL interaction in E3 ...[more]