title: Structure and function of ABC transporters.
abstract: ATP binding cassette transporters are ubiquitous integral membrane proteins that actively transport ligands across biological membranes, a process critical for most aspects of cell physiology. These proteins are important clinically and economically. Their dysfunction underlies a number of human genetic diseases, and the ability of some to pump cytotoxic molecules from cells confers resistance to antibiotics, herbicides, and chemotherapeutic drugs. Recent structure analyses interpreted in light of a large body of biochemistry has resulted in the ATP-switch model for function in which the paired nucleotide binding domains switch between an ATP-dependent closed conformation and a nucleotide-free, open conformation to drive the translocation of ligand.
authors.affiliation: MRC Clinical Sciences Centre, Imperial College Hammersmith Hospital Campus, London, United Kingdom. kenneth.linton@csc.mrc.ac.uk
authors.forename: Kenneth J
authors.initials: KJ
authors.lastname: Linton
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000737:chemistry* / Q000502:physiology*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001693:Biological Transport, Active / Q000502:physiology; D002352:Carrier Proteins / Q000502:physiology; D006801:Humans; D008024:Ligands; D009711:Nucleotides / Q000378:metabolism; D011487:Protein Conformation; D017434:Protein Structure, Tertiary / Q000502:physiology
chemical_list: D018528:ATP-Binding Cassette Transporters; D002352:Carrier Proteins; D008024:Ligands; D009711:Nucleotides; D000255:Adenosine Triphosphate