title: Structure of the multidrug resistance P-glycoprotein.
abstract: In order to elucidate the mechanism by which the multidrug resistance P-glycoprotein extrudes cytotoxic drugs from the cell, and particularly the number and nature of the drug binding site(s), knowledge of the structure of P-gp is essential. A considerable body of genetic and biochemical data has accrued which gives insights into P-gp structure and function. These data are critically reviewed, particularly in relation to the low resolution structure of P-gp which has recently been determined by electron microscopy. P-gp is one of the best characterised of the ABC transporters and these structure-function studies may have more general implications.
authors.affiliation: Nuffield Department of Clinical Biochemistry, University of Oxford, John Radcliffe Hospital, UK.
authors.forename: C F
authors.initials: CF
authors.lastname: Higgins
authors.forename: R
authors.initials: R
authors.lastname: Callaghan
authors.forename: K J
authors.initials: KJ
authors.lastname: Linton
authors.forename: M F
authors.initials: MF
authors.lastname: Rosenberg
authors.forename: R C
authors.initials: RC
authors.lastname: Ford
mesh_terms: D020168:ATP Binding Cassette Transporter, Subfamily B, Member 1 / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D006801:Humans; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
chemical_list: D020168:ATP Binding Cassette Transporter, Subfamily B, Member 1