Abstract

ATP-Binding Cassette (ABC) transporters constitute one of the largest superfamily of transmembrane proteins, present in both prokaryotes and eukaryotes. ATP hydrolysis at the nucleotide binding domains (NBD) drives conformational changes in the transmembrane domains (TMD) allowing substrate translocation. During this process, the structure of the ABC transporter alternates between the inward-facing (IF) conformation and the outward-facing (OF) conformation. The most prevalent and best characterized ABC-member is the mammalian P-glycoprotein (Pgp).

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