The yeast Pdr5p multidrug transporter: How does it recognize so many substrates?

Multidrug transporters are of considerable importance because they present problems in the treatment of infectious disease and cancer. A central issue is the ability of efflux pumps to recognize an astounding array of structurally diverse compounds. The yeast Pdr5p efflux pump, which is a member of...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2007-04, Vol.356 (1), p.1-5
Main Authors: Golin, John, Ambudkar, Suresh V., May, Leopold
Format: Article
Language:English
Subjects:
ABC transporter
ATP-Binding Cassette Transporters - chemistry
ATP-Binding Cassette Transporters - metabolism
Binding Sites
Binding, Competitive
Biological Transport
Hydrophobic and Hydrophilic Interactions
Imidazoles - chemistry
Imidazoles - metabolism
Pdr5
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - metabolism
Substrate Specificity
Yeast multidrug resistance
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Summary:Multidrug transporters are of considerable importance because they present problems in the treatment of infectious disease and cancer. A central issue is the ability of efflux pumps to recognize an astounding array of structurally diverse compounds. The yeast Pdr5p efflux pump, which is a member of the ATP-binding cassette superfamily, has at least 3 substrate-binding sites, each of which appears to use different chemical properties to transport compounds. All Pdr5p substrates, however, have a size requirement that is independent of hydrophobicity.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2007.02.011