ABCB1 p.Thr199Arg
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PMID: 17848563
[PubMed]
Loo TW et al: "Suppressor mutations in the transmembrane segments of P-glycoprotein promote maturation of processing mutants and disrupt a subset of drug-binding sites."
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7
The presence of arginine residues reduced the apparent affinity of P-gp for vinblastine (L65R, T199R, and I306R), cyclosporin (I306R and F343R), or rhodamine B (F343R) by 4-60-fold.
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ABCB1 p.Thr199Arg 17848563:7:95
status: NEW69 For disulfide cross-linking analysis, the cDNA of mutant L339C(TM6)/ F728C(TM7) (34) was modified to also encode the L65R, T199R, I306R, or F343R mutations.
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ABCB1 p.Thr199Arg 17848563:69:123
status: NEW164 Effect of L65R and T199R Mutations on Maturation of a P-gp Processing Mutant-We then tested whether arginines introduced into TM1 (Leu65 ) (27) or TM3 (Thr199 ) promoted maturation of a P-gp processing mutant.
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ABCB1 p.Thr199Arg 17848563:164:19
status: NEW271 It is possible, however, that residue 199 lies some distance away from the actual rhodamine B binding site because the T199R mutation did not reduce the apparent affinity for rhodamine B in the cross-linking protection assay (Table 1).
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ABCB1 p.Thr199Arg 17848563:271:119
status: NEW273 The residue at position 199 in TM3, however, does appear to lie close to the vinblastine-binding site because the T199R mutation reduced the apparent affinity for vinblastine by 6.4-fold (Table 1).
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ABCB1 p.Thr199Arg 17848563:273:114
status: NEW