The ABC transporter structure and mechanism: Perspectives on recent research

Publication Type:
Journal Article
Cellular and Molecular Life Sciences, 2004, 61 (6), pp. 682 - 699
Issue Date:
Filename Description Size
Thumbnail2004000812.pdf2.02 MB
Adobe PDF
Full metadata record
ATP-binding cassette (ABC) transporters are multidomain integral membrane proteins that utilise the energy of ATP hydrolysis to translocate solutes across cellular membranes in all phyla. ABC transporters form one of the largest of all protein families and are central to many important biomedical phenomena, including resistance of cancers and pathogenic microbes to drugs. Elucidation of the structure and mechanism of ABC transporters is essential to the rational design of agents to control their function. While a wealth of high-resolution structures of ABC proteins have been produced in recent years, many fundamental questions regarding the protein's mechanism remain unanswered. In this review, we examine the recent structural data concerning ABC transporters and related proteins in the light of other experimental and theoretical data, and discuss these data in relation to current ideas concerning the transporters' molecular mechanism.
Please use this identifier to cite or link to this item: