ABCC7 p.Thr1057Cys
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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.Thr1057Cys 18658148:90:108
status: NEW101 B, T966C/E543C at the CL3/NBD1 interface and T1057C/E543C at the CL4/NBD1 interface at the X-loop of NBD1.
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ABCC7 p.Thr1057Cys 18658148:101:45
status: NEW142 To determine whether the interfacial interaction of Glu-543 with CL3 and CL4 was indeed affected by PKA phosphorylation, membrane vesicles from HEK cells overexpressing Cys-less CFTR with Cys pairs E543C/T966C and E543C/T1057C were pretreated with PKA in the presence of ATP and Mg2ϩ before cross-linking with various MTS reagents.
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ABCC7 p.Thr1057Cys 18658148:142:220
status: NEW143 As shown in Fig. 4A, similar to the experiments with whole cells in membranes not treated with PKA, the Cys pairs E543C/T966C and E543C/T1057C were cross-linked by all the MTS reagents tested.
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ABCC7 p.Thr1057Cys 18658148:143:136
status: NEW