ABCC7 p.Leu172Cys
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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."
No.
Sentence
Comment
90
Cys pair cross-linking experiments showed that indeed E543C could be cross-linked with both T966C (CL3) and T1057C (CL4, Fig. 2B), while D1341C was in close contact with both L172C (CL1) and N268C (CL2, Fig. 2C).
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ABCC7 p.Leu172Cys 18658148:90:175
status: NEW102 C, L172C/D1341C at the CL1/NBD2 interface and N268C/D1341C at the CL2/NBD2 interface at the X-loop of NBD2.
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ABCC7 p.Leu172Cys 18658148:102:3
status: NEW127 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.Leu172Cys 18658148:127:64
status: NEW173 On the other hand, the cross-linking between L172C of CL1 and D1341C of NBD2 rapidly and reversibly inhibited channel gating (Fig. 6D) very similar to what we had observed previously for the CL2/NBD2 interface (19).
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ABCC7 p.Leu172Cys 18658148:173:45
status: NEW174 However, in the case of the completely reversible cessation of gating caused by L172C/D1341C cross-linking, the role of modification of each of these cysteines individually will have to be studied in detail because treatment with monofunctional MTSES also inhibited gating.
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ABCC7 p.Leu172Cys 18658148:174:80
status: NEW