ABCC7 p.Thr1064Cys
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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
81
In addition to the Phe-508-containing NBD1 surface patch, residues in other regions of the domain also interact with CL4 residues as evidenced by cross-linking of Cys pairs involving amino acids closer to the Q loop (Gln-493), including W496C/T1064C and M498C/L1065C as well as nearer the Walker B motif (Asp-572) such as K564C/G1069C (Fig. 3A and SI Fig. 8).
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ABCC7 p.Thr1064Cys 18305154:81:243
status: NEW97 Phe-508 participates in an apparent aromatic cluster with residues from CL4(seealsoSIFig.10).CL4alsointeractswithotherregionsinNBD1assuggested by cross-linking of residues close to the Q loop (W496C/T1064C and M498C/ L1065C) and a residue near the Walker B motif (K564C/G1069C).
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ABCC7 p.Thr1064Cys 18305154:97:199
status: NEW
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
80
In agreement with what is predicted by our model, we were able to cross-link residue pairs W496C/T1064C, M498C/L1065C (19), which proves that indeed CL4 also interacts with NBD1 through the so called Q-loop (Q493).
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ABCC7 p.Thr1064Cys 18658148:80:97
status: NEW159 Membrane vesicles prepared from HEK cells transiently transfected with Cys pairs introduced at E543C with T966C (CL3) and T1064C (CL4) were pretreated with PKA catalytic subunit in the presence of ATP before incubating with 20 M MTS reagents.
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ABCC7 p.Thr1064Cys 18658148:159:122
status: NEW