ABCC3 p.Thr1237Gly
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PMID: 12924948
[PubMed]
Zhang DW et al: "Characterization of the role of polar amino acid residues within predicted transmembrane helix 17 in determining the substrate specificity of multidrug resistance protein 3."
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Sentence
Comment
75
They are as follows: S1229A (5'-GGG CTG GTG GGG CTA GCT GTG TCC TAC TCC-3'), S1231A (5'-GC CTT TCT GTG GCC TAC TCC CTG CAG GTG ACA-3'), Y1232F (5'-T TCT GTG TCC TTC TCC TTA CAG GTG ACA TTT G-3'), S1233A (5'-CT GTG TCC TAC GCC CTG CAG GTG ACA TTT G-3'), Q1235A (5'-G TCC TAC TCC TTG GCG GTG ACA TTT GCT C-3'), T1237A (5'-CC TTG CAG GTG GCA TTC GCT CTG AAC TGG-3'), T1237S (5'-CC TTG CAG GTG TCC TTC GCT CTG AAC TGG-3'), T1237G (5'-CC TTG CAG GTG GGA TTC GCT CTG AAC TGG-3'), T1237L (5'-CC TTG CAG GTG CTA TTC GCT CTG AAC TGG-3'), and N1241A (5'-GTG ACA TTT GCG CTA GCC TGG ATG ATA C-3').
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ABCC3 p.Thr1237Gly 12924948:75:419
status: NEW189 Effect of Mutations T1237G, T1237S, and T1237L on VP-16 Resistance.
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ABCC3 p.Thr1237Gly 12924948:189:20
status: NEW193 As shown in Table 2, mutation T1237G, like T1237A, significantly FIGURE 4: ATP-dependent [3H]E217βG uptake by membrane vesicles prepared from HEK293 cells stably transfected with wild-type or mutant MRP3. Panel A: Relative protein expression levels of wild-type and mutant MRP3 proteins in stably transfected HEK293 cells.
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ABCC3 p.Thr1237Gly 12924948:193:30
status: NEW210 Effects of Mutations T1237G, T1237S, and T1237L on the Transport Profile of MRP3.
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ABCC3 p.Thr1237Gly 12924948:210:21
status: NEW212 Thus, the effects of the mutations T1237G, T1237S, and T1237L on the ability of MRP3 to transport these three substrates were also examined by in vitro transport assays (Figure 8B-D).
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ABCC3 p.Thr1237Gly 12924948:212:35
status: NEW213 Replacement of Thr1237 with Gly, like mutation T1237A, dramatically increased the ability of MRP3 to transport methotrexate (Figure 8B), E217βG (Figure 8C), and taurocholate (Figure 8D).
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ABCC3 p.Thr1237Gly 12924948:213:15
status: NEW278 Although the majority of mutations that eliminated hydrogen-bonding potential had a negative effect on the activity FIGURE 8: Effect of mutations T1237S, T1237L, and T1237G on ATP-dependent [3H]methotrexate (panel B), [3H]E217βG (panel C), and [3H]taurocholate (panel D) uptake by wild-type MRP3.
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ABCC3 p.Thr1237Gly 12924948:278:166
status: NEW288 In addition, conversion of polar residue Thr1237 to either Ala or Gly markedly increased the ability to confer VP-16 resistance and to transport E217βG, taurocholate, and methotrexate, while mutation to a bulkier and more hydrophobic Leu residue resulted in only a moderate increase in transport of all three substrates.
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ABCC3 p.Thr1237Gly 12924948:288:41
status: NEW