ABCB1 p.Ser979Cys

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PMID: 9261097 [PubMed] Loo TW et al: "Drug-stimulated ATPase activity of human P-glycoprotein requires movement between transmembrane segments 6 and 12."
No. Sentence Comment
68 To test these predictions, we introduced pairs of cysteines into a Cys-less mutant of P-glycoprotein to create the mutants F336C/S979C, L339C/V982C, F343C/M986C, G346C/G989C, and P350C/S993C.
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ABCB1 p.Ser979Cys 9261097:68:129
status: NEW
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78 No cross-linked product was observed for mutants F336C/S979C and L339C/V982C.
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ABCB1 p.Ser979Cys 9261097:78:55
status: NEW
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80 We also tested mutants F335C/L976C, L339C/S979C, F343C/F983C, G347C/A987C, and S351C/ V991C for cross-linking since they were predicted to lie on opposing faces of TM6 and TM12 modeled in a right-handed coiled-coil.
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ABCB1 p.Ser979Cys 9261097:80:42
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107 Mutants S979C/F336C or L339C/V982C did not yield any cross-linked product even in the presence of ATP or drug substrates (data not shown).
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ABCB1 p.Ser979Cys 9261097:107:8
status: NEW
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124 Cross-linking was not observed between F336C/S979C or L339C/V982C, even in the presence of ATP or drug substrates FIG. 2.
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ABCB1 p.Ser979Cys 9261097:124:45
status: NEW
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PMID: 9841738 [PubMed] Jones PM et al: "A new structural model for P-glycoprotein."
No. Sentence Comment
211 In contrast, two other potential pairs that lie between the first and second of the four cross-linked pairs within TMs 6 and 12 (Loo & Clarke, 1997), namely F336C/S979C and L339C/V982C, failed to form cross-links.
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ABCB1 p.Ser979Cys 9841738:211:163
status: NEW
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