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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.
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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.
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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.
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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.
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