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The ATP-binding cassette (ABC) superfamily of transport systems now includes over thirty proteins that share extensive sequence similarity and domain organization. This superfamily includes the well characterized periplasmic binding protein-dependent uptake systems of prokaryotes, bacterial exporters, and eukaryotic proteins including the P-glycoprotein associated with multidrug resistance in tumours (MDR), the STE6 gene product that mediates export of yeast a-factor mating pheromone, pfMDR that is implicated in chloroquine resistance of the malarial parasite, and the product of the cystic fibrosis gene (CFTR). Here we present a tertiary structure model of the ATP-binding cassettes characteristic of this class of transport system, based on similarities between the predicted secondary structures of members of this family and the previously determined structure of adenylate kinase. This model has implications for both the molecular basis of transport and cystic fibrosis and provides a framework for further experimentation.

Original publication

DOI

10.1038/346362a0

Type

Journal article

Journal

Nature

Publication Date

26/07/1990

Volume

346

Pages

362 - 365

Keywords

ATP Binding Cassette Transporter, Subfamily B, Member 1, Adenosine Triphosphate, Amino Acid Sequence, Animals, Carrier Proteins, Cystic Fibrosis, Drosophila, Drug Resistance, Escherichia coli, Humans, Membrane Glycoproteins, Models, Molecular, Molecular Sequence Data, Neoplasm Proteins, Protein Conformation, Salmonella typhimurium, Sequence Homology, Nucleic Acid