ABCMdb

ABCC3 p.Thr1237Leu

None has been submitted yet.

Publications

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."

No. 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'). Login to comment
189 Effect of Mutations T1237G, T1237S, and T1237L on VP-16 Resistance. Login to comment
201 Substitution of Thr1237 with Leu only moderately enhanced resistance to VP-16. Login to comment
210 Effects of Mutations T1237G, T1237S, and T1237L on the Transport Profile of MRP3. Login to comment
212 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). Login to comment
278 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. Login to comment