Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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ATP Binding Cassette Transporter, Subfamily B, Member 1 / chemistry
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ATP Binding Cassette Transporter, Subfamily B, Member 1 / metabolism
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ATP-Binding Cassette Transporters / chemistry
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ATP-Binding Cassette Transporters / metabolism
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Bacterial Proteins / chemistry
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Bacterial Proteins / metabolism
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Cryoelectron Microscopy
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Humans
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In Vitro Techniques
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Models, Biological
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Models, Molecular
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Multidrug Resistance-Associated Proteins / chemistry*
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Multidrug Resistance-Associated Proteins / metabolism*
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Multidrug Resistance-Associated Proteins / ultrastructure
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Protein Conformation
Substances
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ATP Binding Cassette Transporter, Subfamily B, Member 1
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ATP-Binding Cassette Transporters
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Bacterial Proteins
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MsbA protein, Bacteria
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Multidrug Resistance-Associated Proteins