ABCC7 p.Leu408Cys

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PMID: 18658148 [PubMed] He L et al: "Multiple membrane-cytoplasmic domain contacts in the cystic fibrosis transmembrane conductance regulator (CFTR) mediate regulation of channel gating."
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116 Based on the latter model, we attempted to detect cross-linking of the residue pairs V171C/E407C and V171C/L408C in the whole protein, but did not observe any indication of cross-linking of the mature band (supplemental Fig. S2A).
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ABCC7 p.Leu408Cys 18658148:116:107
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119 To test this hypothesis, membrane vesicles were prepared from BHK cells overexpressing Cys-less CFTR containing V171C and L408C.
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ABCC7 p.Leu408Cys 18658148:119:122
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127 No cross-linking was detected when Cys pairs were introduced at L172C/E543C, T966C/D1341C, V171C/L1261C, or M961C/L408C, which are not predicted to be in association in the structural model (supplemental Fig. S3).
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ABCC7 p.Leu408Cys 18658148:127:114
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135 Membrane vesicles prepared from BHK cells overexpressing Cys-less CFTR containing the Cys pair V171C and L408C were treated with 20 ␮M MTS cross-linker M8M before limited trypsin digestion with concentrations indicated in the figures.
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ABCC7 p.Leu408Cys 18658148:135:105
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172 Turning from the effects of cross-linking CL3 to those of its counterpart, CL1 in the N-terminal MSD, its cross-linking to NBD1 i.e. V171C/L408C had essentially no influence on gating (Fig. 6C).
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ABCC7 p.Leu408Cys 18658148:172:139
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203 A, M961C/L1261C at the CL3/NBD2 interface; B, T966C/E543C at the CL3/NBD1 interface; C, V171C/L408C at the CL1/NBD1 interface; D, L171C/D1341C at the CL1/NBD2 interface.
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ABCC7 p.Leu408Cys 18658148:203:94
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244 We have verified the latter conformation by introducing Cys pairs in CL1 and different residues in RI (V171C/ E407C, V171C/L408C) and showing that these pairs can be cross-linked by M8M (Fig. 3B).
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ABCC7 p.Leu408Cys 18658148:244:123
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