ABCC1 p.His827Trp
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PMID: 17187755
[PubMed]
Yang R et al: "Hydrogen-bond formation of the residue in H-loop of the nucleotide binding domain 2 with the ATP in this site and/or other residues of multidrug resistance protein MRP1 plays a crucial role during ATP-dependent solute transport."
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Sentence
Comment
43
In addition, the following mutations as shown in Fig. 5A (H827D, H1486D, H827D/ H1486D, H827N, H1486N, H827N/H1486N, H827E, H1486E, H827E/ H1486E, H827Q, H1486Q, H827Q/H1486Q, H827Y, H1486Y, H827Y/ H1486Y, H827W, H1486W and H827W/H1486W) were also introduced into the full length MRP1 cDNA by using the following primers: H827D/forward, 5'-CGG ATC TTG GTC ACG GAC AGC ATG AGC TAC TTG-3'; H827D/ reverse, 5'-CAA GTA GCT CAT GCT GTC CGT GAC CAA GAT CCG-3'; H1486D/forward, 5'-GTC CTC ACC ATC GCC GAC CGG CTC AAC ACC ATC-3'; H1486D/reverse, 5'-GAT GGT GTT GAG CCG GTC GGC GAT GGT GAG GAC-3'; H827N/forward, 5'-CGG ATC TTG GTC ACG AAC AGC ATG AGC TAC TTG-3'; H827N/reverse, 5'-CAA GTA GCT CAT GCT GTT CGT GAC CAA GAT CCG-3'; H1486N/forward, 5'-GTC CTC ACC ATC GCC AAC CGG CTC AAC ACC ATC-3'; H1486N/reverse, 5'-GAT GGT GTT GAG CCG GTT GGC GAT GGT GAG GAC-3'; H827E/forward, 5'-CGG ATC TTG GTC ACG GAG AGC ATG AGC TAC TTG-3'; H827E/reverse, 5'-CAA GTA GCT CAT GCT CTC CGT GAC CAA GAT CCG-3'; H1486E/forward, 5'-GTC CTC ACC ATC GCC GAG CGG CTC AAC ACC ATC-3'; H1486E/reverse, 5'-GAT GGT GTT GAG CCG CTC GGC GAT GGT GAG GAC-3'; H827Q/forward, 5'- CGG ATC TTG GTC ACG CAG AGC ATG AGC TAC TTG-3'; H827Q/ reverse, 5'-CAA GTA GCT CAT GCT CTG CGT GAC CAA GAT CCG-3'; H1486Q/forward, 5'-GTC CTC ACC ATC GCC CAG CGG CTC AAC ACC ATC-3'; H1486Q/reverse, 5'-GAT GGT GTT GAG CCG CTG GGC GAT GGT GAG GAC-3'; H827Y/forward, 5'-CGG ATC TTG GTC ACG TAC AGC ATG AGC TAC TTG-3'; H827Y/reverse, 5'-CAA GTA GCT CAT GCT GTA CGT GAC CAA GAT CCG-3'; H1486Y/forward, 5'-GTC CTC ACC ATC GCC TAC CGG CTC AAC ACC ATC-3'; H1486Y/reverse, 5'-GAT GGT GTT GAG CCG GTA GGC GAT GGT GAG GAC-3'; H827W/forward, 5'-CGG ATC TTG GTC ACG TGG AGC ATG AGC TAC TTG-3'; H827W/reverse, 5'-CAA GTA GCT CAT GCT CCA CGT GAC CAA GAT CCG-3'; H1486W/forward, 5'-GTC CTC ACC ATC GCC TGG CGG CTC AAC ACC ATC-3'; H1486W/reverse, 5'-GAT GGT GTT GAG CCG CCA GGC GAT GGT GAG GAC-3'.
X
ABCC1 p.His827Trp 17187755:43:206
status: NEWX
ABCC1 p.His827Trp 17187755:43:224
status: NEWX
ABCC1 p.His827Trp 17187755:43:1655
status: NEWX
ABCC1 p.His827Trp 17187755:43:1721
status: NEW164 In order to test this hypothesis, H827D, H1486D, H827D/H1486D, H827N, H1486N, H827N/H1486N, H827E, H1486E, H827E/H1486E, H827Q, H1486Q, H827Q/H1486Q, H827Y, H1486Y, H827Y/ H1486Y, H827W, H1486W and H827W/H1486W mutations (Fig. 5A) were introduced into full length of MRP1 cDNA in pNUT/MRP1/His and expressed in BHK cells at 37 °C.
X
ABCC1 p.His827Trp 17187755:164:180
status: NEWX
ABCC1 p.His827Trp 17187755:164:198
status: NEW166 Consistent with the H827L or H827F mutation in NBD1, all of the NBD1 mutants, including H827D, H827N, H827E, H827Q, H827Y and H827W, have transport activities similar to that of wild-type MRP1 (Fig. 5C), implying that no matter whether or not these NBD1 mutants form hydrogen-bonds with these components, none of them has a significant effect on the ATP hydrolysis at the un-mutated NBD2 and the ATP-dependent solute transport.
X
ABCC1 p.His827Trp 17187755:166:126
status: NEW190 H827L-, H827F-, H827D-, H827N-, H827E-, H827Q-, H827Y- and H827W-mutated MRP1 form complex glycosylated mature protein in BHK cells at 37 °C (Figs. 4A and 5B), implying that these mutations in NBD1 did not significantly alter the protein conformation.
X
ABCC1 p.His827Trp 17187755:190:59
status: NEW