ABCC1 p.Asp793Gln
[switch to full view]Comments [show]
None has been submitted yet.
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.
X
ABCC1 p.Asp793Gln 12882957:78:24
status: NEW248 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).
X
ABCC1 p.Asp793Gln 12882957:248:109
status: NEW251 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.
X
ABCC1 p.Asp793Gln 12882957:251:26
status: NEW264 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).
X
ABCC1 p.Asp793Gln 12882957:264:57
status: NEW267 Although labeling at NBD2 was decreased in the D793Q and D793N mutants, this domain remained the predominant site of photolabeling (Fig. 8B, lanes 7 and 9).
X
ABCC1 p.Asp793Gln 12882957:267:47
status: NEW270 Effect of D793Q, D793N, D793S, E1455S, E1455Q, E1455N, E1455L mutations on [3 H]LTC4 transport activity.
X
ABCC1 p.Asp793Gln 12882957:270:10
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.
X
ABCC1 p.Asp793Gln 12882957:271:119
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."
X
ABCC1 p.Asp793Gln 12882957:275:55
status: NEW304 Comparison of nucleotide binding and vanadate trapping by wild-type MRP1 and mutant proteins (D793Q, D793N, D793S, E1455S, E1455Q, E1455N, and E1455L).
X
ABCC1 p.Asp793Gln 12882957:304:94
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.
X
ABCC1 p.Asp793Gln 12882957:305:98
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.
X
ABCC1 p.Asp793Gln 12882957:308:276
status: NEW339 Mutation of Asp793 to Asn, Gln, and also Ser, which is the residue found at the comparable position of cystic fibrosis transmembrane conductance regulator, all decreased slightly LTC4 transport activity, whereas the comparable mutations of Glu1455 inactivated the protein (Fig. 7B).
X
ABCC1 p.Asp793Gln 12882957:339:12
status: NEW