Dataset Information
Cryo Electron Microscopy micrographs of Inward-facing, ligand-free MRP2
Ontology highlight
ABSTRACT:
SUBMITTER: Jue Chen
PROVIDER: EMPIAR-13617 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structural basis for the transport and regulation mechanism of the multidrug resistance-associated protein 2.
Nature communications 20250108 1
Multidrug resistance-associated protein 2 (MRP2) is an ATP-powered exporter important for maintaining liver homeostasis and a potential contributor to chemotherapeutic resistance. Using cryogenic electron microscopy (cryo-EM), we determine the structures of human MRP2 in three conformational states: an autoinhibited state, a substrate-bound pre-translocation state, and an ATP-bound post-translocation state. In the autoinhibited state, the cytosolic regulatory (R) domain plugs into the transmembr ...[more]