ABCMdb

ABCC3 p.Ser1233Ala

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

8 Mutations Y1232F and S1233A reduced resistance to VP-16 and the transport of all three substrates tested. Login to 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
138 Replacement of Ser1229 with Ala had no significant effect on MRP3-mediated E217βG uptake, whereas mutations S1231A, Y1232F, S1233A, Q1235A, and N1241A all decreased the transport activity. Login to comment
146 However, mutations S1229A, S1231A, Y1232F, S1233A, and N1241A all reduced methotrexate transport activity. Login to comment
150 However, mutations Y1232F and S1233A both decreased taurocholate transport activity by approximately 30-50%. Login to comment
186 However, mutation of five hydrophilic amino acid residues (S1231A, Y1232F, S1233A, Q1235A, and N1241A) caused approximately a 2-3-fold reduction of resistance to VP-16. Login to comment
188 Thus, on the basis of the substrates tested in this study, mutations S1229A, S1231A, Q1235A, and N1241A affected substrate specificity of MRP3, whereas mutations Y1232F, S1233A, and T1237A influenced the overall activity of the protein. Login to comment