Journal
PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY
Volume 453, Issue 5, Pages 555-567Publisher
SPRINGER HEIDELBERG
DOI: 10.1007/s00424-006-0126-x
Keywords
ABC transporter; nucleotide-binding domain; transmembrane domain; ATP switch; ATP hydrolysis; P-glycoprotein; drug resistance
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Funding
- Medical Research Council [MC_U120088463] Funding Source: researchfish
- MRC [MC_U120088463] Funding Source: UKRI
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ATP-binding cassette (ABC) transporters are ubiquitous integral membrane proteins that facilitate the transbilayer movement of ligands. They comprise, minimally, two transmembrane domains, which impart ligand specificity, and two nucleotide-binding domains (NBDs), which power the transport cycle. Almost 25 years of biochemistry is reviewed in light of the recent structure analyses resulting in the ATP-switch model for function in which the NBDs switch between a dimeric conformation, closed around two molecules of ATP, and a nucleotide-free, dimeric 'open' conformation. The flexibility of this switching mechanism has evolved to provide different kinetic control for different transporters and has also been co-opted to diverse functions other than transmembrane transport.
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