title: Similarities between ATP-dependent and ion-coupled multidrug transporters.
abstract: The movement of drugs across biological membranes is mediated by two major classes of membrane transporters. Primary-active, ABC (ATP-binding cassette) multidrug transporters are dependent on ATP-binding/hydrolysis, whereas secondary-active multidrug transporters are coupled to the proton (or sodium)-motive force that exists across the plasma membrane. Recent work on LmrA, an ABC multidrug transporter in Lactococcus lactis, suggests that primary- and secondary-active multidrug transporters share functional and structural features. Some of these similarities and their implications for the mechanism of transport by ABC multidrug transporters will be discussed.
authors.affiliation: Department of Pharmacology, University of Cambridge, Cambridge CB2 1PD, UK.
authors.forename: H
authors.initials: H
authors.lastname: Venter
authors.forename: S
authors.initials: S
authors.lastname: Shahi
authors.forename: L
authors.initials: L
authors.lastname: Balakrishnan
authors.forename: S
authors.initials: S
authors.lastname: Velamakanni
authors.forename: A
authors.initials: A
authors.lastname: Bapna
authors.forename: B
authors.initials: B
authors.lastname: Woebking
authors.forename: H W
authors.initials: HW
authors.lastname: van Veen
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism*; D017920:Antiporters / Q000378:metabolism; D018432:Drug Resistance, Multiple; D026901:Membrane Transport Proteins / Q000378:metabolism; D027425:ATP-Binding Cassette, Sub-Family C Proteins / Q000378:metabolism*
chemical_list: D000255:Adenosine Triphosphate; D017920:Antiporters; D026901:Membrane Transport Proteins; D027425:ATP-Binding Cassette, Sub-Family C Proteins