ABCB1 p.Tyr1087Cys
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PMID: 18708637
[PubMed]
Loo TW et al: "Processing mutations disrupt interactions between the nucleotide binding and transmembrane domains of P-glycoprotein and the cystic fibrosis transmembrane conductance regulator (CFTR)."
No.
Sentence
Comment
151
Because no cross-linking studies have identified cysteines that could be cross-linked at the TMD1-NBD2 interface, we constructed a series of double cysteine mutants between a cysteine in TMD1 (A266C or F267C) and another in NBD2 (R1085C, F1086C, Y1087C or D1088C) that would be equivalent to L443C(NBD1) and S909C(TMD2), respectively, in each half of P-gp.
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ABCB1 p.Tyr1087Cys 18708637:151:246
status: NEW
PMID: 23733192
[PubMed]
Loo TW et al: "Human P-glycoprotein contains a greasy ball-and-socket joint at the second transmission interface."
No.
Sentence
Comment
121
To test whether the F1086C mutation inhibited folding, the F1086C mutant and the Y1087C mutant were expressed in the absence of drug substrates.
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ABCB1 p.Tyr1087Cys 23733192:121:81
status: NEW122 The Y1087C mutant was included because an aromatic residue at position 1087 is highly conserved in ABC proteins (17).
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ABCB1 p.Tyr1087Cys 23733192:122:4
status: NEW123 It was found that both the F1086C and the Y1087C mutations inhibited maturation of Cys-less P-gp (Fig. 3D).
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ABCB1 p.Tyr1087Cys 23733192:123:42
status: NEW