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Multidrug resistance ABC transporters.
1Department of Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd. CB-105, La Jolla, CA 92037, USA. gchang@scripps.edu
FEBS Letters
|November 25, 2003
Summary
Multidrug resistance proteins, specifically ATP binding cassette (ABC) transporters, efflux drugs and lipids using ATP. This review details their structures and proposes a transport mechanism linked to ATP hydrolysis.
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Biology
Background:
- Clinical multidrug resistance is mediated by integral membrane proteins.
- ATP binding cassette (ABC) transporters are a key class of these proteins, involved in efflux of hydrophobic drugs and lipids.
Purpose of the Study:
- To review the structures and conformational changes of multidrug resistance ABC transporters.
- To propose a general mechanism for substrate transport coupled to ATP hydrolysis.
Main Methods:
- Literature review of existing biochemical and structural data.
- Analysis of structure-function relationships in ABC transporters.
Main Results:
- Detailed examination of multidrug resistance ABC transporter structures.
- Identification of key conformational changes during transport.
- Proposed mechanism for ATP-dependent drug/lipid efflux.
Conclusions:
- Multidrug resistance ABC transporters utilize ATP hydrolysis to drive the efflux of hydrophobic substrates.
- Understanding these mechanisms is crucial for developing strategies to overcome drug resistance.