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Multidrug resistance ABC transporters
Author(s) -
Chang Geoffrey
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01085-8
Subject(s) - atp binding cassette transporter , efflux , multiple drug resistance , permease , transporter , atp hydrolysis , multidrug resistance associated proteins , membrane transport protein , multidrug resistance associated protein 2 , biochemistry , membrane transport , chemistry , transport protein , integral membrane protein , cell membrane , drug resistance , biology , membrane protein , membrane , enzyme , atpase , gene , microbiology and biotechnology , antibiotics
Clinical multidrug resistance is caused by a group of integral membrane proteins that transport hydrophobic drugs and lipids across the cell membrane. One class of these permeases, known as multidrug resistance ATP binding cassette (ABC) transporters, translocate these molecules by coupling drug/lipid efflux with energy derived from the hydrolysis of ATP. In this review, we examine both the structures and conformational changes of multidrug resistance ABC transporters. Together with the available biochemical and structural evidence, we propose a general mechanism for hydrophobic substrate transport coupled to ATP hydrolysis.