ABCC1 p.Leu1430Arg
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PMID: 15152943
[PubMed]
Szentpetery Z et al: "Functional studies on the MRP1 multidrug transporter: characterization of ABC-signature mutant variants."
No.
Sentence
Comment
46
The conserved leucines of the LSGGQ motifs were replaced by arginines (L768R, L1430R) and the conserved glycines in the fourth position of the signature motifs were substituted for aspartic acids (G771D, G1433D).
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ABCC1 p.Leu1430Arg 15152943:46:78
status: NEW122 In Figure 2 we document that, when measuring the ATPase activity of the L768R and L1430R signature mutants, we found that they possessed a significant level of vanadate-sensitive, drug-stimulated ATPase activity.
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ABCC1 p.Leu1430Arg 15152943:122:82
status: NEW128 As shown in Figure 3, in harmony with the ATPase activity measurements, the L768R and L1430R signature mutants presented 87-89 % of the transport activity of the wild-type MRP1, while the G771D and G1433D signature mutants had only a negligible level of ATP-dependent LTC4 uptake, similar to that found in the ‚-galactosidase- expressing control membranes.
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ABCC1 p.Leu1430Arg 15152943:128:86
status: NEW129 All these functional studies indicated that the catalytic cycles of the L768R and L1430R mutants were similar to the wild-type, while that of the G771D and G1433D mutants were seriously diminished.
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ABCC1 p.Leu1430Arg 15152943:129:82
status: NEW172 We chose leucine, a residue not oriented towards the ATP, which we substituted for arginine (L768R, L1430R).
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ABCC1 p.Leu1430Arg 15152943:172:100
status: NEW178 We found that the ATPase and transport activity of the L768R and L1430R signature mutants, reflecting the whole catalytic cycle of MRP1, were not significantly different from that of the wild-type MRP1.
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ABCC1 p.Leu1430Arg 15152943:178:65
status: NEW
PMID: 15252017
[PubMed]
Szentpetery Z et al: "The role of the conserved glycines of ATP-binding cassette signature motifs of MRP1 in the communication between the substrate-binding site and the catalytic centers."
No.
Sentence
Comment
184
These mutations affect the conserved LSGGQ motifs in either ABC domain; the leucines were replaced with arginines (L768R and L1430R), and the glycines in position 4 were substituted with glutamic acids (G771D and G1433D).
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ABCC1 p.Leu1430Arg 15252017:184:125
status: NEW
PMID: 17295059
[PubMed]
Chang XB et al: "A molecular understanding of ATP-dependent solute transport by multidrug resistance-associated protein MRP1."
No.
Sentence
Comment
181
Mutation of the first residue in LSGGQ signature sequence to an R residue, L768R in NBD1 or L1430R in NBD2, retained both ATPase activity and ATP-dependent solute transport activity [116], indicating that this L residue is not crucial for the NBD1·ATP2·NBD2 sandwich structure formation.
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ABCC1 p.Leu1430Arg 17295059:181:92
status: NEW