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lüll Fungal PDR transporters: Phylogeny, topology, motifs and function Lamping E; Baret PV; Holmes AR; Monk BC; Goffeau A; Cannon RDFungal Genet Biol 2010[Feb]; 47 (2): 127-42The overexpression of pleiotropic drug resistance (PDR) efflux pumps of the ATP-binding cassette (ABC) transporter superfamily frequently correlates with multidrug resistance. Phylogenetic analysis of 349 full-size ( approximately 160kDa) PDR proteins (Pdrps) from 55 fungal species, including major fungal pathogens, identified nine separate protein clusters (A-G, H1a/H1b and H2). Fungal, plant and human ABCG-family Pdrps possess a nucleotide-binding domain [NBD] and a transmembrane domain [TMD] in a family-defining 'reverse' ABC transporter topology [NBD-TMD] that is duplicated [NBD-TMD](2) in full-size fungal and plant Pdrps. Although full-size Pdrps have similar halves indicating early gene duplication/fusion, they show asymmetry of their NBDs and extracellular loops (ELs). Members of cluster F are most symmetric and may be closely related to the evolutionary ancestor of Pdrps. Unique structural elements are predicted, new PDR-specific motifs identified, and the significance of these and other structural features discussed.|*Phylogeny[MESH]|ATP-Binding Cassette Transporters/chemistry/metabolism/physiology[MESH]|Amino Acid Motifs[MESH]|Antifungal Agents/pharmacology[MESH]|DNA-Binding Proteins/chemistry[MESH]|Drug Resistance, Fungal/genetics/*physiology[MESH]|Drug Resistance, Multiple/genetics/*physiology[MESH]|Fungal Proteins/*chemistry/metabolism/*physiology[MESH]|Fungi/*classification/metabolism/*physiology[MESH]|Humans[MESH] |