ABCC1 p.Asp793Ser

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Publications
PMID: 12882957 [PubMed] Payen LF et al: "Role of carboxylate residues adjacent to the conserved core Walker B motifs in the catalytic cycle of multidrug resistance protein 1 (ABCC1)."
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78 The forward primers for D793Q, D793N, D793S, E1455Q, E1455N, E1455S, and E1455L were 5Ј-GCTGACATTTACCTCTTCGATCAACCGCTCTC- AGCAGTGGATGCC-3Ј, 5Ј-GCTGACATTTACCTCTTCGATAATCCGC- TCTCAGCAGTGGATGCC-3Ј, 5Ј-GCTGACATTTACCTCTTCGATTCT- CCCCTCTCAGCAGTGGATGCC-3Ј, 5Ј-CGAAGATCCTTGTGTTGGA- TCAGGCCACGGCGGCCGTGGACCTGG-3Ј, 5Ј-CGAAGATCCTTGTG- TTGGATA ACGCCACGGCCGCCGTGGACCTGG-3Ј, 5Ј-CGAAGATCC- TTGTGTTGGATTCGGCCACGGCAGCCGTGGACCTGG-3Ј, 5Ј-CGAA- GATCCTTGTGTTGGATTTGGCCACGGCCGCCGTGGACCTGG-3Ј, respectively.
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ABCC1 p.Asp793Ser 12882957:78:38
status: NEW
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248 Unlike the D793E mutation, which decreased LTC4 transport activity by 80%, NBD1 mutations (D793S, D793N, and D793Q) had little effect on ATP-dependent LTC4 uptake (Fig. 7B).
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ABCC1 p.Asp793Ser 12882957:248:91
status: NEW
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251 At 4 °C, mutation of Asp793 to Ser, Gln, or Asn decreased photolabeling of NBD1 by 8-azido-[␣-32 P]ATP to a similar extent.
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ABCC1 p.Asp793Ser 12882957:251:26
status: NEW
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264 Similar to wild-type, in the absence of vanadate, D793S, D793Q, and D793N mutant proteins did not display any nucleotide binding at either NBD (Fig. 8B).
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ABCC1 p.Asp793Ser 12882957:264:50
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266 In the presence of vanadate, the labeling profile of the D793S mutation was very similar to wild-type with nucleotide being bound relatively strongly by NBD2 (Fig. 8B, lanes 3 and 5).
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ABCC1 p.Asp793Ser 12882957:266:57
status: NEW
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270 Effect of D793Q, D793N, D793S, E1455S, E1455Q, E1455N, E1455L mutations on [3 H]LTC4 transport activity.
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ABCC1 p.Asp793Ser 12882957:270:24
status: NEW
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271 A, membrane proteins (1 ␮g) from Sf21 cells expressing both halves of either MRP1 (MRP1 dh) or mutant proteins (D793Q, D793N, D793S, E1455S, E1455Q, E1455N, E1455L) were separated by SDS-PAGE on gradient gels and transferred to Immobilon-P membranes.
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ABCC1 p.Asp793Ser 12882957:271:133
status: NEW
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275 B, membrane vesicles (2 ␮g) containing MRP1 dh, D793Q, D793S, D793N, E1455Q, E1455S, E1455N, E1455L, or beta-Gus were assayed for ATP-dependent LTC4 transport activity at 23 °C for up to 3 min in transport buffer containing [3 H]LTC4 (50 nM, 0.13 ␮Ci), as described under "Experimental Procedures."
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ABCC1 p.Asp793Ser 12882957:275:62
status: NEW
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304 Comparison of nucleotide binding and vanadate trapping by wild-type MRP1 and mutant proteins (D793Q, D793N, D793S, E1455S, E1455Q, E1455N, and E1455L).
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ABCC1 p.Asp793Ser 12882957:304:108
status: NEW
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305 A, at 4 °C, 8-azido- [␣-32 P]ATP photolabeling by wild-type MRP1 and mutant proteins (D793Q, D793N, D793S, E1455S, E1455Q, E1455N, and E1455L) was evaluated. Membrane vesicles (20 ␮g) were incubated with 5 ␮M 8-azido-[␣-32 P]ATP for 5 min on ice in transport buffer containing 5 mM MgCl2.
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ABCC1 p.Asp793Ser 12882957:305:112
status: NEW
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308 The position of the labeled MRP1 NH2-half and COOH-half polypeptides are indicated, and endogenous proteins labeled are indicated by E followed by arrows. B and C, at 37 °C under trapping conditions, 8-azido-[␣-32 P]ADP trapping by wild-type MRP1 mutant proteins (D793Q, D793N, D793S, E1455S, E1455Q, E1455N, and E1455L) was studied.
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ABCC1 p.Asp793Ser 12882957:308:290
status: NEW
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