In-Between-RING (IBR) of Human Parkin

The IBR domain of Parkin has been shown to increase binding of the E2 proteins UbcH7 and UbcH8 subsequently causing the ubiquitination of synphilin-1, Sept5, and SIM2. The structure of Parkin along with mutational data creates a proposed model showing the IBR domain as a facilitator for the arrangement of the adjacent RING1 and RING2 domains.


Authors
Beasley, S.A., Hristova, V.A., Shaw, G.S.
Title
Structure of Parkin in-between-ring domain provides insights for E3-ligase dysfunction in autosomal recessive Parkinson's disease.
Journal (PubMed)

PDB ID (PDB)