Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain

B. Ward, Andrew; Szewczyk, Paul; Grimard, Vinciane; Lee, Chang‐Wook; Martinez, Lorena; Doshi, Rupak; Caya, Alexandra; Villaluz, Mark; Pardon, Els; Cregger, Cristina; J. Swartz, Douglas; Falson, Pierre; L. Urbatsch, Ina; Govaerts, Cédric; Steyaert, Jan; Chang, Geoffrey

doi:10.1073/pnas.1309275110

Public

Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain

Published in Proceedings of the National Academy of Sciences • Jul 30, 2013

Authors:

Andrew B. Ward

Paul Szewczyk

Vinciane Grimard

Abstract

P-glycoprotein (P-gp) is one of the best-known mediators of drug efflux-based multidrug resistance in many cancers. This validated therapeutic target is a prototypic, plasma membrane resident ATP-Binding Cassette transporter that pumps xenobiotic compounds out of cells. The large, polyspecific drug-...

Subject

Epitope

ATP-binding cassette transporter

Cyclic nucleotide-binding domain

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