ABCC7 p.Met961Cys
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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
106
To confirm these contacts in the case of CL3 and NBD2, we designed several Cys pairs from CL3 (M961C and S962C) and NBD2 (L1260C and L1261C) (Fig. 3A).
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ABCC7 p.Met961Cys 18658148:106:95
status: NEW108 In constructs containing the Cys pairs M961C/L1261C (Fig. 3A), M961C/L1260C, and S962C/ L1261C (supplemental Fig. S1A), MTS reagent treatment produced a slightly, albeit distinguishably, faster moving band, which could be reversed by DTT.
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ABCC7 p.Met961Cys 18658148:108:39
status: NEWX
ABCC7 p.Met961Cys 18658148:108:63
status: NEW111 Cross-linking of Cys pairs between CL3 and NBD2 was also confirmed with co-expression of constructs of Cys-less ⌬NBD2 CFTR containing M961C together with the Cys-less NBD2 fragment containing L1261C in HEK cells (supplemental Fig. S1, B and C).
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ABCC7 p.Met961Cys 18658148:111:141
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.Met961Cys 18658148:127:108
status: NEW156 First, cross-linking between residues M961C and L1261C at the CL3/ NBD2 interface changed channel gating behavior substantially but did not arrest it completely (Fig. 6A).
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ABCC7 p.Met961Cys 18658148:156:38
status: NEW203 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.Met961Cys 18658148:203:3
status: NEW