ABCC7 p.Val1147Cys
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PMID: 21796338
[PubMed]
Qian F et al: "Functional arrangement of the 12th transmembrane region in the CFTR chloride channel pore based on functional investigation of a cysteine-less CFTR variant."
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Sentence
Comment
62
b Example leak subtracted I-V relationships for N1138C, T1142C, V1147C, and N1148C, recorded from inside out membrane patches following maximal channel activation with PKA, ATP, and PPi.
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ABCC7 p.Val1147Cys 21796338:62:64
status: NEW64 As described in the text, whereas MTSES application always led to a decrease in macroscopic current amplitude in reactive mutants, the effects of MTSET were to decrease (e.g., N1138C, V1147C), increase (e.g., T1142C) or not significantly alter (e.g., N1148C) macroscopic current amplitude.
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ABCC7 p.Val1147Cys 21796338:64:184
status: NEW80 Application of MTSES (200 μM) or MTSET (2 mM) to the intracellular solution after channel activation with PKA, ATP, and PPi significantly altered macroscopic current amplitude in nine out of 19 cysteine-substituted mutants tested (N1138C, M1140C, S1141C, T1142C, Q1144C, W1145C, V1147C, N1148C, and S1149C; Figs. 1 and 2).
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ABCC7 p.Val1147Cys 21796338:80:285
status: NEW86 However, unlike previous findings in TM6 [9], we observed a third pattern for cysteines introduced closest to the putative cytoplasmic end of TM12 (V1147C, N1148C, and S1149C).
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ABCC7 p.Val1147Cys 21796338:86:148
status: NEW87 Here, macroscopic current amplitude was decreased by MTSES application but either decreased (V1147C, S1149C) or not significantly affected (N1148C) by MTSET application.
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ABCC7 p.Val1147Cys 21796338:87:93
status: NEW
PMID: 25143385
[PubMed]
El Hiani Y et al: "Metal bridges illuminate transmembrane domain movements during gating of the cystic fibrosis transmembrane conductance regulator chloride channel."
No.
Sentence
Comment
51
To investigate potential Cd2af9; bridges formed between pore-lining cysteine side chains exposed in the inner vestibule of the CFTR pore, we combined individual cysteines that we previously found to be accessible to cytoplasmically applied methanethiosulfonate reagents in three important pore-lining TMs: TM1 (K95C, Q98C) (13), TM6 (I344C, V345C, M348C, A349C) (15), and TM12 (M1140C, S1141C, T1142C, Q1144C, W1145C, V1147C, N1148C) (16), to generate a total of 50 double cysteine mutants (8 TM1:TM6; 14 TM1:TM12; 28 TM6:TM12).
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ABCC7 p.Val1147Cys 25143385:51:421
status: NEW71 In contrast, the remaining seven double cysteine mutants, namely I344C/S1141C (Fig. 2, C and D), V345C/S1141C, M348C/ S1141C (Fig. 2, C and E), M348C/V1144C, M348C/W1145C, M348C/V1147C, and M348C/N1148C, all showed increased sensitivity to Cd2af9; , leading to a significant decrease in Ki as compared with either of the single cysteine mutants from which they were derived (estimated Ki values b0d; 50 òe;M; Fig. 3).
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ABCC7 p.Val1147Cys 25143385:71:178
status: NEW137 Thus, M348C is able to form Cd2af9; bridges with cysteines at multiple positions in TM12 (S1141C, Q1144C, W1145C, V1147C, N1148C) (Fig. 8B), and S1141C is able to form Cd2af9; bridges with cysteines both in TM1 (K95C) and in TM6 (I344C, V345C, M348C) (Fig. 8C).
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ABCC7 p.Val1147Cys 25143385:137:117
status: NEW