ABCB3 p.Val656Ala
| Predicted by SNAP2: | A: N (57%), C: N (72%), D: D (75%), E: D (71%), F: D (66%), G: D (66%), H: D (66%), I: N (87%), K: D (71%), L: N (87%), M: N (57%), N: D (66%), P: D (75%), Q: D (66%), R: D (71%), S: N (66%), T: N (78%), W: D (75%), Y: D (71%), |
| Predicted by PROVEAN: | A: D, C: D, D: D, E: D, F: D, G: D, H: D, I: N, K: D, L: N, M: N, N: D, P: D, Q: D, R: D, S: D, T: D, W: D, Y: D, |
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[hide] The multidrug transporter Pdr5 on the 25th anniver... Biochem J. 2015 May 1;467(3):353-63. doi: 10.1042/BJ20150042. Golin J, Ambudkar SV
The multidrug transporter Pdr5 on the 25th anniversary of its discovery: an important model for the study of asymmetric ABC transporters.
Biochem J. 2015 May 1;467(3):353-63. doi: 10.1042/BJ20150042., [PMID:25886173]
Abstract [show]
Asymmetric ABC (ATP-binding cassette) transporters make up a significant proportion of this important superfamily of integral membrane proteins. These proteins contain one canonical (catalytic) ATP-binding site and a second atypical site with little enzymatic capability. The baker's yeast (Saccharomyces cerevisiae) Pdr5 multidrug transporter is the founding member of the Pdr subfamily of asymmetric ABC transporters, which exist only in fungi and slime moulds. Because these organisms are of considerable medical and agricultural significance, Pdr5 has been studied extensively, as has its medically important homologue Cdr1 from Candida albicans. Genetic and biochemical analyses of Pdr5 have contributed important observations that are likely to be applicable to mammalian asymmetric ABC multidrug transporter proteins, including the basis of transporter promiscuity, the function of the non-catalytic deviant ATP-binding site, the most complete description of an in vivo transmission interface, and the recent discovery that Pdr5 is a molecular diode (one-way gate). In the present review, we discuss the observations made with Pdr5 and compare them with findings from clinically important asymmetric ABC transporters, such as CFTR (cystic fibrosis transmembrane conductance regulator), Cdr1 and Tap1/Tap2.
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No. Sentence Comment
161 Our group also constructed and tested a V656A mutant and showed that it was clearly signal-deficient.
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ABCB3 p.Val656Ala 25886173:161:40
status: NEW163 The V656A mutant had a phenotype that was nearly identical with that of S558Y, including an ATPase that was reduced relative to WT, but markedly resistant to allosteric inhibition by clotrimazole (5-fold as resistant as the WT).
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ABCB3 p.Val656Ala 25886173:163:4
status: NEW200 Therefore these mutants altered the stimulation signal, much like S558Y, V656L and V656A altered the trans-inhibition of Pdr5 ATPase by clotrimazole [18-20].
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ABCB3 p.Val656Ala 25886173:200:83
status: NEW245 The mutant phenotype was therefore much like those of other signalling mutants, such as S558Y and V656A.
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ABCB3 p.Val656Ala 25886173:245:98
status: NEW