Cellular and Molecular Life Sciences

, Volume 66, Issue 19, pp 3111–3126

The ATP-binding cassette family: a structural perspective

Authors

  • Veronica Kos
    • Department of Molecular and Cellular Biology, College of Biological SciencesUniversity of Guelph
    • Faculty of Life Sciences, Manchester Interdisplinary BiocentreThe University of Manchester
Review

DOI: 10.1007/s00018-009-0064-9

Cite this article as:
Kos, V. & Ford, R.C. Cell. Mol. Life Sci. (2009) 66: 3111. doi:10.1007/s00018-009-0064-9

Abstract

The ATP-binding cassette family is one of the largest groupings of membrane proteins, moving allocrites across lipid membranes, using energy from ATP. In bacteria, they reside in the inner membrane and are involved in both uptake and export. In eukaryotes, these transporters reside in the cell’s internal membranes as well as in the plasma membrane and are unidirectional—out of the cytoplasm. The range of substances that these proteins can transport is huge, which makes them interesting for structure–function studies. Moreover, their abundance in nature has made them targets for structural proteomics consortia. There are eight independent structures for ATP-binding cassette transporters, making this one of the best characterised membrane protein families. Our understanding of the mechanism of transport across membranes and membrane protein structure in general has been enhanced by recent developments for this family.

Keywords

ATP-binding cassetteMembrane proteinStructureTransporterLipid bilayer

Copyright information

© Birkhäuser Verlag, Basel/Switzerland 2009