期刊
FEBS JOURNAL
卷 277, 期 3, 页码 540-549出版社
WILEY
DOI: 10.1111/j.1742-4658.2009.07485.x
关键词
ABCB1; ABC transporter; ATP hydrolysis; kinetic substrate selection; ligand binding; multidrug efflux; multidrug resistance; Pdr5; TAP; transport mechanism
资金
- EMBO Long Term Fellowship [ALTF 379-2008]
- DFG [1279/2-3, 1279/5-3]
- Austrian Science Foundation [SFB035-04]
- Austrian Science Fund (FWF) [F 3504] Funding Source: researchfish
Multidrug resistance is a major challenge in the therapy of cancer and pathogenic fungal infections. More than three decades ago, P-glycoprotein was the first identified multidrug transporter. It has been studied extensively at the genetic and biochemical levels ever since. Pdr5, the most abundant ATP-binding cassette transporter in Saccharomyces cerevisiae, is highly homologous to azole-resistance-mediating multidrug transporters in fungal pathogens, and a focus of clinical drug resistance research. Despite functional equivalences, P-glycoprotein and Pdr5 exhibit striking differences in their architecture and mechanisms. In this minireview, we discuss the mechanisms of substrate selection and multidrug transport by comparing the fraternal twins P-glycoprotein and Pdr5. We propose that substrate selection in eukaryotic multidrug ATP-binding cassette transporters is not solely determined by structural features of the transmembrane domains but also by their dynamic behavior.
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