ABCMdb

ABCC1 p.Gly771Ala

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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

66 The forward primers for the G771A and G1433A mutations of signature sequences were 5Ј-CCTGTCT- GGGGCCCAGAAGCAGC-3Ј and 5Ј-CCTCAGTGTCGCGCAGCGC- CAG-3Ј, respectively. Login to comment
196 The G771A and G1433A mutants were expressed at 90 and 50%, respectively, of the level of wt MRP1. Login to comment
198 In contrast to the results obtained with the Walker A and B mutants, the NBD1 ABC signature mutation G771A eliminated LTC4 transport, whereas the NBD2 G1433A mutant retained approximately 30% of the activity of the wt protein (Fig. 7B). Login to comment
200 Under vanadate-induced trapping conditions, both of the G771A and G1433A mutations markedly decreased the trapping of ADP at NBD2 but had relatively little effect on the low level of trapping typically observed at NBD1 (Fig. 7D). Login to comment
276 A, expression levels of wt and G771A and G1433A mutant MRP1 half-molecules. Login to comment
278 The relative expression levels of wt and mutant proteins were evaluated by densitometry and are indicated in the figure. B, effect of G771A and G1433A mutations on ATP-dependent LTC4 transport activity. Login to comment
279 Membrane vesicles (2 ␮g) containing wt and the G771A and G1433A 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
280 Similar results were obtained in three additional independent experiments. C, effect of G771A and G1433A mutations on photolabeling with 8-azido-[␥-32 P]ATP. Login to comment
284 D, effect of G771A and G1433A mutations on vanadate-dependent nucleotide trapping. Login to comment
291 Membrane vesicles (50 ␮g of total protein) containing wt and the G771A and G1433A 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

28 Accordingly, mutations of the residues that should interact with the γ-phosphate of the bound ATP [28,29], such as K1333M [19] or G771A [30], also almost abolished the ATP-dependent solute transport activity completely. 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

183 Accordingly, the mutants at these positions, such as G771D, G771A, G1433D or G1433A, did not lose their ability to bind ATP, but significantly reduced their Vi-dependent nucleotide trapping at 37°C [61, 116, 117]. Login to 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: 18636743 [PubMed] Yang R et al: "Interaction between the bound Mg.ATP and the Walker A serine residue in NBD2 of multidrug resistance-associated protein MRP1 plays a crucial role for the ATP-dependent leukotriene C4 transport."

No. Sentence Comment

182 The reduced nucleotide binding at the mutated NBD2, such as S1334A, S1334C, S1334D, S1334H, and S1334N, significantly decreased the ability to inhibit the LTC4 binding (Figure 7), similar to the mutations of K684E, G771A, or K1333E (19). 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

145 However, substitution of the conserved glycine residue at the fourth position of LSGGQ motif with an A or a D residue in NBD1 (G771D or G771A) or in NBD2 (G1433D or G1433A) lost their abilities to transport substrate across the membrane (99, 151, 152). Login to 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