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Nature


Title:"Structural model of ATP-binding proteins associated with cystic fibrosis, multidrug resistance and bacterial transport"
Author(s):Hyde SC; Emsley P; Hartshorn MJ; Mimmack MM; Gileadi U; Pearce SR; Gallagher MP; Gill DR; Hubbard RE; Higgins CF;
Address:"Imperial Cancer Research Fund Laboratories, University of Oxford, John Radcliffe Hospital, UK"
Journal Title:Nature
Year:1990
Volume:346
Issue:6282
Page Number:362 - 365
DOI: 10.1038/346362a0
ISSN/ISBN:0028-0836 (Print) 0028-0836 (Linking)
Abstract:"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"
Keywords:"ATP Binding Cassette Transporter, Subfamily B, Member 1 Adenosine Triphosphate/*metabolism Amino Acid Sequence Animals Carrier Proteins/*genetics/metabolism Cystic Fibrosis/genetics/metabolism Drosophila/genetics/metabolism Drug Resistance/*genetics Esche;"
Notes:"MedlineHyde, S C Emsley, P Hartshorn, M J Mimmack, M M Gileadi, U Pearce, S R Gallagher, M P Gill, D R Hubbard, R E Higgins, C F eng Comparative Study Research Support, Non-U.S. Gov't England 1990/07/26 Nature. 1990 Jul 26; 346(6282):362-5. doi: 10.1038/346362a0"

 
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