ABCC1 p.Glu1455Asn
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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)."
No.
Sentence
Comment
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.Glu1455Asn 12882957:78:53
status: NEW241 To determine whether there may be additional consequences to eliminating the carboxylate side chain, we mutated Asp793 and Glu1455 to Asn, Gln, and Ser as observed in cystic fibrosis transmembrane conductance regulator.
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ABCC1 p.Glu1455Asn 12882957:241:123
status: NEW249 In contrast, the NBD2 mutations (E1455S, E1455N, E1455Q, and E1455L) like E1455D completely abolished LTC4 transport (Fig. 7B).
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ABCC1 p.Glu1455Asn 12882957:249:41
status: NEW254 Mutation to Ser, Gln, and Leu essentially eliminated labeling of NBD2, whereas labeling of the E1455N mutation was similar to that of the FIG. 6.
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ABCC1 p.Glu1455Asn 12882957:254:95
status: NEW268 Like the E1455D mutant, the E1455S, E1455N, and E1455L mutations resulted in strong vanadate-independent photolabeling of NBD2 and increased vanadate-dependent photolabeling of NBD1 (Fig. 8C, lanes 3, 4, and 7-10).
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ABCC1 p.Glu1455Asn 12882957:268:36
status: NEW270 Effect of D793Q, D793N, D793S, E1455S, E1455Q, E1455N, E1455L mutations on [3 H]LTC4 transport activity.
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ABCC1 p.Glu1455Asn 12882957:270:47
status: NEW271 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.Glu1455Asn 12882957:271:156
status: NEW275 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.Glu1455Asn 12882957:275:92
status: NEW304 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.Glu1455Asn 12882957:304:131
status: NEW305 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.Glu1455Asn 12882957:305:135
status: NEW308 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.Glu1455Asn 12882957:308:313
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
261
This conclusion is further supported by mutation of the putative catalytic residue E1455 in NBD2 that all the mutants, including E1455S, E1455Q, E1455N, E1455L and E1455D, lost their abilities to transport LTC4 across membrane bilayer [62, 144].
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ABCC1 p.Glu1455Asn 17295059:261:145
status: NEW