title: The yeast Pdr5p multidrug transporter: how does it recognize so many substrates?
abstract: Multidrug transporters are of considerable importance because they present problems in the treatment of infectious disease and cancer. A central issue is the ability of efflux pumps to recognize an astounding array of structurally diverse compounds. The yeast Pdr5p efflux pump, which is a member of the ATP-binding cassette superfamily, has at least 3 substrate-binding sites, each of which appears to use different chemical properties to transport compounds. All Pdr5p substrates, however, have a size requirement that is independent of hydrophobicity.
authors.affiliation: Department of Biology, The Catholic University of America, Washington, DC 20064, USA. golin@cua.edu
authors.forename: John
authors.initials: J
authors.lastname: Golin
authors.forename: Suresh V
authors.initials: SV
authors.lastname: Ambudkar
authors.forename: Leopold
authors.initials: L
authors.lastname: May
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D001667:Binding, Competitive; D001692:Biological Transport; D057927:Hydrophobic and Hydrophilic Interactions; D007093:Imidazoles / Q000737:chemistry / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D018528:ATP-Binding Cassette Transporters; D007093:Imidazoles; C092438:PDR5 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; C029899:imidazole