ABCD1 p.Trp326Ala
| Predicted by SNAP2: | A: D (63%), C: D (63%), D: D (80%), E: D (75%), F: N (57%), G: D (71%), H: D (66%), I: D (63%), K: D (75%), L: D (59%), M: D (63%), N: D (66%), P: D (75%), Q: D (66%), R: D (66%), S: D (66%), T: D (71%), V: D (63%), Y: N (57%), |
| Predicted by PROVEAN: | A: D, C: D, D: D, E: D, F: D, G: D, H: D, I: D, K: D, L: D, M: D, N: D, P: D, Q: D, R: D, S: D, T: D, V: D, Y: D, |
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[hide] Yeast ATP-Binding Cassette Transporters Conferring... Annu Rev Microbiol. 2012 Oct 13;66:39-63. Epub 2012 Jun 11. Prasad R, Goffeau A
Yeast ATP-Binding Cassette Transporters Conferring Multidrug Resistance.
Annu Rev Microbiol. 2012 Oct 13;66:39-63. Epub 2012 Jun 11., [PMID:22703054]
Abstract [show]
Overexpression of the ATP-binding cassette (ABC) drug transporter P-glycoprotein (P-gp) is often responsible for the failure of chemotherapy as a treatment for human tumors. The presence of proteins homologous to P-gp in organisms ranging from prokaryotes to eukaryotes indicates that drug export is a general mechanism of multidrug resistance. Yeasts are no exception. They have developed a large subfamily of ABC exporters involved in pleiotropic drug resistance (PDR) and in the cellular efflux of a wide variety of drugs. The PDR transporters Pdr5p of Saccharomyces cerevisiae and Cdr1p of Candida albicans are important members of this PDR subfamily, which comprises up to 10 phylogenetic clusters in fungi. Here, we review current achievements concerning the structure, molecular mechanism, and physiological functions of yeast Pdr transporters.
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No. Sentence Comment
1022 Thus, the mutant Trp326Ala remains capable of ATP hydrolysis; however, it does so with a much higher KM value, indicating that the docking of the substrate in the binding pocket has been altered by the mutation.
X
ABCD1 p.Trp326Ala 22703054:1022:17
status: NEW1023 The protein, however, appears capable of near-normal drug-transport function in cells expressing the full-length protein carrying the Trp326Ala substitution.
X
ABCD1 p.Trp326Ala 22703054:1023:134
status: NEW