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Revision as of 20:55, 26 September 2010

Background Information

ATP-binding cassette (ABC) transporters are a superfamily of integral membrane proteins that harness the energy of ATP binding and hydrolysis to drive the trans-membrane movement of a variety of small molecules. ABC transporters function as homodimers, in which ATP binding and hydrolysis occurs in two sites that the interface of the nucleotide binding domains (NBD), while the paired transmembrane domains (TMD) facilitate substrate transport. Substrates may be imported or exported, depending upon the structure of the transporter. In ABC importers, which have only been found in prokaryotes, the NBD and TMD are separate polypeptides; however, in the ubiquitous exporters, the NBD and TMD are fused.

ABC transporters are of particular medical interest, as they may contribute to the pathogenicity and drug resistance of pathogenic bacteria and some cancers.[1]

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