Ontology highlight
ABSTRACT:
SUBMITTER: Schiffer JM
PROVIDER: S-EPMC4972691 | biostudies-literature | 2016 Aug
REPOSITORIES: biostudies-literature
Schiffer Jamie M JM Malmstrom Robert D RD Parnell Jonathan J Ramirez-Sarmiento Cesar C Reyes Javiera J Amaro Rommie E RE Komives Elizabeth A EA
Structure (London, England : 1993) 20160707 8
Cullin-RING E3 ligases (CRLs) are elongated and bowed protein complexes that transfer ubiquitin over 60 Å to proteins targeted for proteasome degradation. One such CRL contains the ankyrin repeat and SOCS box protein 9 (ASB9), which binds to and partially inhibits creatine kinase (CK). While current models for the ASB9-CK complex contain some known interface residues, the overall structure and precise interface of the ASB9-CK complex remains unknown. Through an integrative modeling approach, we ...[more]