ABCMdb

ABCC1 p.Asp792Asn

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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

67 The forward primers for the D792N and D1454N mutations of the Walker B motifs were 5Ј-CATTTACCTCT- TCAATGATCCCCTC-3Ј and 5Ј-ATCCTTGTGTTGAATGAGGCCA- CG-3Ј, respectively. Login to comment
189 The D792N mutation diminished transport activity by approximately 65%, whereas the D1454N mutation essentially inactivated the protein (Fig. 5B). Login to comment
190 As observed with the NBD1 Walker A mutations, the D792N mutation drastically decreased binding by NBD1 and, to a lesser extent, binding by NBD2. Login to comment
192 The D792N mutation also strongly decreased ADP trapping by both NBD1 and NBD2, although the D1454N mutation eliminated trapping by NBD2 but only modestly decreased trapping by NBD1 (Fig. 6B). Login to comment
193 Despite the partial retention of vanadate-dependent trapping at NBD2 of the D792N mutant, we were unable to detect an ATP/vanadate-dependent decrease in LTC4 binding with either mutant (Fig. 6C). Login to comment
228 The relative expression levels of wt and mutant half-molecules were evaluated by densitometry and are indicated on the figure. B, effect of D792N and D1454N mutations on ATP-dependent LTC4 transport activity. Login to comment
229 Membrane vesicles (2 ␮g) containing wt and the D792N and D1454N mutant MRP1 half-molecules or control beta-gus were assayed for ATP-dependent LTC4 transport activity by incubation in transport buffer containing [3 H]LTC4 (50 nM, 0.13 ␮Ci) at 23°C for 2 min in the presence and absence of ATP (4 mM) as described under Materials and Methods. Results shown are means Ϯ S.D. of triplicate determinations in a single experiment. Login to comment
230 Similar results were obtained in three additional independent experiments. C, effect of D792N and D1454N mutations on photolabeling with 8-azido-[␣-32 P]ATP. Login to comment
242 The effect of the MRP1 Walker B D792N and D1454N mutations on ATP binding and ADP trapping was similar to that of the Walker A lysine mutations; the level of transport activity of the NBD1 aspartic acid-to-asparagine mutation was comparable with that of the Walker A lysine-to-methionine mutation (Gao et al., 2000). Login to comment
260 B, effect of D792N and D1454N mutations on vanadate-dependent nucleotide trapping. Login to comment
265 C, effect of D792N and D1454N mutations on LTC4 photolabeling in the presence or absence of nucleotide. Login to comment
266 Membrane vesicles (50 ␮g of total protein) containing wt and the D792N and D1454N 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: 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

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