Structure and Mechanism of ABC Transporters

Curr Opin Struct Biol. 2002 Dec;12(6):754-60. doi: 10.1016/s0959-440x(02)00399-8.

Abstract

ATP-binding cassette (ABC) transporters are central to many physiological processes, including the uptake of nutrients, the non-classical secretion of signaling molecules and toxins, multidrug resistance and the development of human disease. As one might expect from this spectrum of translocation events, these ubiquitous, ATP-dependent pumps or channels are capable of transporting an enormous variety of substrates, ranging from small ions to large proteins. Recently determined structures of full-length ABC transporters and isolated ABC domains have increased our understanding of the functional mechanism of these proteins.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • ATP-Binding Cassette Transporters / chemistry*
  • ATP-Binding Cassette Transporters / genetics
  • ATP-Binding Cassette Transporters / metabolism*
  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Biological Transport / physiology
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Quaternary
  • Sequence Alignment

Substances

  • ATP-Binding Cassette Transporters
  • Bacterial Proteins