Novel features in the structure of P-glycoprotein (ABCB1) in the post-hydrolytic state as determined at 7.9 Å resolution.
Nopnithi ThonghinRichard F CollinsAlessandro BarbieriTalha ShafiAlistair SiebertRobert C FordPublished in: BMC structural biology (2018)
The structural data imply that (i) a low basal ATPase activity is ensured by steric blockers of NBD dimerization and (ii) allocrite access to the central cavity may be structurally linked to NBD dimerization, giving insights into the mechanism of drug-stimulation of P-glycoprotein activity.