4.7 Review

The ABC transporter structure and mechanism: perspectives on recent research

Journal

CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 61, Issue 6, Pages 682-699

Publisher

SPRINGER BASEL AG
DOI: 10.1007/s00018-003-3336-9

Keywords

ABC transporter; ABC-ATPase; membrane transport; nucleotide-binding domain; ATP hydrolysis; mechanism; P-glycoprotein

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.7
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available