Dataset Information
Cryo-EM structure of nucleotide-free rMRP2
Ontology highlight
ABSTRACT:
SUBMITTER: Konstantinos Beis
PROVIDER: EMPIAR-11893 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structural basis for the modulation of MRP2 activity by phosphorylation and drugs.
Nature communications 20240304 1
Multidrug resistance-associated protein 2 (MRP2/ABCC2) is a polyspecific efflux transporter of organic anions expressed in hepatocyte canalicular membranes. MRP2 dysfunction, in Dubin-Johnson syndrome or by off-target inhibition, for example by the uricosuric drug probenecid, elevates circulating bilirubin glucuronide and is a cause of jaundice. Here, we determine the cryo-EM structure of rat Mrp2 (rMrp2) in an autoinhibited state and in complex with probenecid. The autoinhibited state exhibits ...[more]
