Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 35, Issue 1, Pages 36-42Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2009.07.009
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Funding
- Biotechnology and Biological Sciences Research Council (BBSRC)
- Jasper L. and Jack Denton Wilson Foundation
- US Army [W81XWH05-1-0316]
- NIH [GM61905]
- Skaggs Chemical Biology Foundation
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM061905] Funding Source: NIH RePORTER
- Biotechnology and Biological Sciences Research Council [BB/F008333/1] Funding Source: researchfish
- Medical Research Council [G0401165] Funding Source: researchfish
- BBSRC [BB/F008333/1] Funding Source: UKRI
- MRC [G0401165] Funding Source: UKRI
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Multidrug ABC transporters can transport a wide range of drugs from the cell. Ongoing studies of the prototype mammalian multidrug resistance ATP-binding cassette transporter P-glycoprotein (ABCB1) have revealed many intriguing functional and biochemical features. However, a gap remains in our knowledge regarding the molecular basis of its broad specificity for structurally unrelated ligands. Recently, the first crystal structures of ligand-free and ligand-bound ABCB1 showed ligand binding in a cavity between its two membrane domains, and earlier observations on polyspecificity can now be interpreted in a structural context. Comparison of the new ABCB1 crystal structures with structures of bacterial homologs suggests a critical role for an axial rotation of transmembrane helices for high-affinity binding and low-affinity release of ligands during transmembrane transport.
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