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Curr Opin Struct Biol. 2002 Dec;12(6):754-60.

Structure and mechanism of ABC transporters.

Author information

1
Institute of Biochemistry, Biocenter, Goethe-University Frankfurt, Marie-Curie Strasse 9, Germany. lschmitt@em.uni-frankfurt.de

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.

PMID:
12504680
[Indexed for MEDLINE]

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