PMID: 10581363

Ueda K, Matsuo M, Tanabe K, Morita K, Kioka N, Amachi T
Comparative aspects of the function and mechanism of SUR1 and MDR1 proteins.
Biochim Biophys Acta. 1999 Dec 6;1461(2):305-13., [PubMed]
Sentences
No. Mutations Sentence Comment
465 ABCB1 p.Cys431Ala
X
ABCB1 p.Cys431Ala 10581363:465:108
status: NEW
view ABCB1 p.Cys431Ala details
ABCB1 p.Cys1074Ala
X
ABCB1 p.Cys1074Ala 10581363:465:114
status: NEW
view ABCB1 p.Cys1074Ala details
8-Azido-ATP binding with the wild-type MDR1 was inhibited by 100 WM NEM, while 8-azido-ATP binding with the C431A/C1074A mutant form was not, suggesting that the cysteines of Walker A motifs in both NBFs are responsible for the e&#a1;ects of NEM on ATP binding. Login to comment
466 ABCB1 p.Cys431Ala
X
ABCB1 p.Cys431Ala 10581363:466:27
status: NEW
view ABCB1 p.Cys431Ala details
8-Azido-ATP binding of the C431A mutant form appeared not to be a&#a1;ected by treatment with 100 WM NEM. Login to comment
467 ABCB1 p.Cys431Ala
X
ABCB1 p.Cys431Ala 10581363:467:108
status: NEW
view ABCB1 p.Cys431Ala details
ABCB1 p.Cys1074Ala
X
ABCB1 p.Cys1074Ala 10581363:467:28
status: NEW
view ABCB1 p.Cys1074Ala details
ABCB1 p.Cys1074Ala
X
ABCB1 p.Cys1074Ala 10581363:467:114
status: NEW
view ABCB1 p.Cys1074Ala details
8-Azido-ATP binding with the wild-type MDR1 was inhibited by 100 WM NEM, while 8-azido-ATP binding with the C431A/C1074A mutant form was not, suggesting that the cysteines of Walker A motifs in both NBFs are responsible for the e¡ects of NEM on ATP binding. Login to comment
468 ABCB1 p.Cys431Ala
X
ABCB1 p.Cys431Ala 10581363:468:27
status: NEW
view ABCB1 p.Cys431Ala details
8-Azido-ATP binding of the C431A mutant form appeared not to be a¡ected by treatment with 100 WM NEM. Login to comment
469 ABCB1 p.Cys1074Ala
X
ABCB1 p.Cys1074Ala 10581363:469:28
status: NEW
view ABCB1 p.Cys1074Ala details
However, ATP-binding to the C1074A mutant form was signi'cantly reduced by the same treatment, similar to the wild-type MDR1. Login to comment