ABCC7 p.Lys1284Cys
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PMID: 18305154
[PubMed]
Serohijos AW et al: "Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function."
No.
Sentence
Comment
72
Cross-linking of C276/Q1280C and C276/K1284C confirms interaction of CL2 and NBD2.
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ABCC7 p.Lys1284Cys 18305154:72:38
status: NEW113 In fact, the Q1280C and K1284C substitutions in NBD2 of Cys-less CFTR containing the native Cys-276 residue in CL2 (illustrated in Fig. 3A, Top Right) enabled cross-linking by all MTS reagents tested.
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ABCC7 p.Lys1284Cys 18305154:113:24
status: NEW
PMID: 20233947
[PubMed]
He L et al: "Restoration of domain folding and interdomain assembly by second-site suppressors of the DeltaF508 mutation in CFTR."
No.
Sentence
Comment
122
As shown in Fig. 3A, when ⌬F508 was introduced into Cys-less CFTR containing pairs 276C/Q1280C or 276C/K1284C at the NBD2/CL2 interface, no mature CFTR was detected, and neither M3M nor M8M (200 M) caused cross-linking of the immature band.
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ABCC7 p.Lys1284Cys 20233947:122:110
status: NEW125 As shown in Fig. 3A, ⌬F508-CFTR maturation was restored as was the cross-linking of the Cys pairs 276C/Q1280C and 276C/ K1284C at NBD2/CL2, as indicated by the slower migration rate of the mature bands in SDS-PAGE in samples treated with M3M and M8M (18).
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ABCC7 p.Lys1284Cys 20233947:125:127
status: NEW