ABCA4 p.Lys429Arg
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PMID: 12586381
[PubMed]
Cai J et al: "Overexpression, purification, and functional characterization of ATP-binding cassette transporters in the yeast, Pichia pastoris."
No.
Sentence
Comment
188
Studies with mutants at homologous positions in the Walker A (K429R/K1072R) and B (D551N/ D1196N) sequence motifs of NBD1 and NBD2 showed that alterations at either position completely inactivate the ATPase activity of P-gp.
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ABCA4 p.Lys429Arg 12586381:188:62
status: NEW211 Under such conditions the trypsin sensitivity profiles of double P-gp mutants K429R/K1072R and D551N/D1196N and of single mutants K429R, K1072R, and D1196N were very similar and clearly distinct from the wild-type protein.
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ABCA4 p.Lys429Arg 12586381:211:78
status: NEWX
ABCA4 p.Lys429Arg 12586381:211:130
status: NEW
PMID: 14596601
[PubMed]
Carrier I et al: "Analysis of catalytic carboxylate mutants E552Q and E1197Q suggests asymmetric ATP hydrolysis by the two nucleotide-binding domains of P-glycoprotein."
No.
Sentence
Comment
124
This is in agreement with previous studies of catalytic residue mutants of the Walker A and B signature motifs (K429R, K1072R, D551N, and D1196N) which severely affect the catalytic activity of mouse Mdr3 but have little effect on the nucleotide-binding affinity of the protein (49).
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ABCA4 p.Lys429Arg 14596601:124:112
status: NEW