ABCC1 p.Lys1333Arg
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PMID: 15755910
[PubMed]
Payen L et al: "Functional interactions between nucleotide binding domains and leukotriene C4 binding sites of multidrug resistance protein 1 (ABCC1)."
No.
Sentence
Comment
65
The forward primers for creating K684R, K684E, K1333R, and K1333E mutations of Walker A motifs were 5Ј-GGCTGCGGAAGGTCGTC- CCTGC-3Ј, 5Ј-GGGCTGCGGAGAGTCGTCCCTGC-3Ј, 5Ј-GGGAGC- TGGGAGGTCGTCCCTGA-3Ј, and 5Ј-GGGAGCTGGGGAGTCGTC- CCTGA-3Ј, respectively.
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ABCC1 p.Lys1333Arg 15755910:65:47
status: NEW131 Densitometry of immunoblots of vesicle proteins indicated that levels of the K684R, K684E, K1333R, and K1333E MRP1 mutants ranged from 30 to 60% those of wt MRP1 (Fig. 3A).
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ABCC1 p.Lys1333Arg 15755910:131:91
status: NEW133 It is noteworthy that the K684R substitution in NBD1 decreased ATP-dependent LTC4 uptake by only 40%, whereas the K1333R mutation in NBD2 reduced transport by approximately 80% (Fig. 2B).
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ABCC1 p.Lys1333Arg 15755910:133:114
status: NEW158 Membrane vesicles (1 g of total protein) prepared from Sf21 cells expressing a combination of a wt and mutant half-molecule containing a K684E, K684R, K1333E, or K1333R mutation were separated by SDS-PAGE on gradient gels and transferred to Immobilon-P membranes.
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ABCC1 p.Lys1333Arg 15755910:158:170
status: NEW163 The relative expression levels of wt and mutant proteins evaluated by densitometry are indicated in the figure. B, effect of K684E, K684R, K1333E, and K1333R mutations on ATP-dependent LTC4 transport activity.
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ABCC1 p.Lys1333Arg 15755910:163:151
status: NEW176 In contrast, both the K1333R and the K1333E mutations essentially eliminated binding at NBD2 but had little or no effect on the labeling of NBD1 (Fig. 3C).
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ABCC1 p.Lys1333Arg 15755910:176:22
status: NEW179 Likewise, both the K1333R and K1333E mutations eliminated trapping by the mutant NBD2 (Fig. 3D).
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ABCC1 p.Lys1333Arg 15755910:179:19
status: NEW204 Membrane vesicles (50 g of total protein) containing wt and the K684R, K684E, K1333R, and K1333E mutant MRP1 half-molecules were incubated in transport buffer at 23°C for 20 min in the absence or presence of ATP␥S (4 mM) or ATP (1 mM) plus vanadate (1 mM) before the addition of [3 H]LTC4 (200 nM, 0.13 Ci).
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ABCC1 p.Lys1333Arg 15755910:204:86
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
241
Indeed, several mutations, such as K684E, K1333E, K684R, K1333R, D792N, D1454N, G771A and G1433A, significantly diminished ATP binding and Vi-dependent ADP trapping at NBD2 and lost the ability to shift the substrate binding from a high to low affinity site [61].
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ABCC1 p.Lys1333Arg 17295059:241:57
status: NEW259 In contrast, mutation of the Walker A motif K1333 residue in NBD2, such as K1333L [40, 141, 148], K1333M [16, 63, 118], K1333R [61] or K1333E [61], mainly affected ATP binding (at 4°C) at the mutated NBD2 [61, 148] and significantly decreased the ATP hydrolysis at the mutated NBD2 [61, 148].
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ABCC1 p.Lys1333Arg 17295059:259:120
status: NEW
PMID: 19949927
[PubMed]
Chang XB et al: "Molecular mechanism of ATP-dependent solute transport by multidrug resistance-associated protein 1."
No.
Sentence
Comment
157
Indeed, several mutations, such as K684E, K1333E, K684R, K1333R, D792N, D1454N, G771A and G1433A, significantly diminished ATP binding and lost the ability to shift the bound substrate from high to low affinity site (99).
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ABCC1 p.Lys1333Arg 19949927:157:57
status: NEW