ABCB1 p.Gly427Cys
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PMID: 12226074
[PubMed]
Loo TW et al: "The "LSGGQ" motif in each nucleotide-binding domain of human P-glycoprotein is adjacent to the opposing walker A sequence."
No.
Sentence
Comment
77
Cross-linking involving residues G427C, N428C, and S434C was not done because the single cysteine mutants, G427C and S434C, showed little or no activity (Ͻ5%), while N428C was defectively processed and rapidly degraded.
X
ABCB1 p.Gly427Cys 12226074:77:33
status: NEWX
ABCB1 p.Gly427Cys 12226074:77:107
status: NEW
PMID: 8995353
[PubMed]
Loo TW et al: "Correction of defective protein kinesis of human P-glycoprotein mutants by substrates and modulators."
No.
Sentence
Comment
64
In addition to the mutants G268V and ⌬Y490, we were able to facilitate processing of P-glycoproteins with mutations in the predicted transmembrane segments (TM1, G54V; TM5, G300V; TM7, A718L; and TM9, A841L), in the extracellular loops between transmembrane segments (G854V), in the cytoplasmic loops (G251V and W803A), in the nucleotide-binding domains (G427C and S434C), and in the linker region connecting the two halves of the molecule (E707A) (data not shown).
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ABCB1 p.Gly427Cys 8995353:64:362
status: NEW
PMID: 9614062
[PubMed]
Loo TW et al: "Superfolding of the partially unfolded core-glycosylated intermediate of human P-glycoprotein into the mature enzyme is promoted by substrate-induced transmembrane domain interactions."
No.
Sentence
Comment
48
Misprocessing mutations are located throughout the molecule; these include the transmembrane domains (e.g. A123L), intracellular (e.g. E243A) and extracellular (e.g. Y853C) loops, the linker region (e.g. E707A), and both nucleotide-binding domains (e.g. G427C, P1194A).
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ABCB1 p.Gly427Cys 9614062:48:254
status: NEW
PMID: 18035039
[PubMed]
Lawson J et al: "Structure-based interpretation of the mutagenesis database for the nucleotide binding domains of P-glycoprotein."
No.
Sentence
Comment
679
Two studies have proposed that the Walker-A cysteine residues can be cross-linked to the opposite Walker-A motif [73,74], either through a direct disulphide between the two naturally occurring Walker-A cysteines [74] or between the Walker-A cysteine of NBD2 and a G427C Walker-A NBD1 mutation [73].
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ABCB1 p.Gly427Cys 18035039:679:264
status: NEW674 Two studies have proposed that the Walker-A cysteine residues can be cross-linked to the opposite Walker-A motif [73,74], either through a direct disulphide between the two naturally occurring Walker-A cysteines [74] or between the Walker-A cysteine of NBD2 and a G427C Walker-A NBD1 mutation [73].
X
ABCB1 p.Gly427Cys 18035039:674:264
status: NEW