ABCMdb

ABCC1 p.Lys684Arg

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Publications

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. Login to comment
131 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). Login to comment
133 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). Login to comment
158 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. Login to comment
163 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. Login to comment
175 The conservative K684R mutation also decreased photolabeling of both NBDs but to a lesser extent than either the aspartic acid or methionine mutations (Fig. 3C). Login to comment
204 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). Login to comment

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."

No. Sentence Comment

189 For example, ATP binding to wild-type MRP1 can transport the bound LTC4 from high to low affinity site whereas ATP binding to the K684R- or the D1454N-mutated MRP1 cannot [30]. Login to comment

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]. Login to comment
256 Mutation of the Walker A motif K684 residue in NBD1, such as K684L [40, 141, 148], K684M [16, 63, 118], K684R [61] or K684E [61], significantly reduced ATP binding (at 4°C) at the mutated NBD1 and the intact NBD2 and Vi dependent ADP trapping at 37°C, but never completely abolished ATP-dependent solute transport. Login to comment
257 In addition, these mutations, such as K684R [61], did not affect LTC4 binding and ATPγS or ATP + Vi did not inhibit LTC4 labeling. Login to comment

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). Login to comment