Removal of the Fe(iii) site promotes activation of the human cystic fibrosis transmembrane conductance regulator by high-affinity Zn(ii) binding

Metallomics ◽  
2018 ◽  
Vol 10 (2) ◽  
pp. 240-247
Author(s):  
Guangyu Wang
Keyword(s):  
Cystic Fibrosis ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Transmembrane Conductance Regulator ◽  
Nucleotide Binding Domain ◽  
Transmembrane Conductance ◽  
High Affinity ◽  
Channel Opening ◽  
Cystic Fibrosis Transmembrane ◽  
Nucleotide Binding Domain 2

High-affinity Zn(ii) bridging C1344 of nucleotide-binding domain 2 (NBD2) with E402 of NBD1, D173 of intracellular loop1 (ICL1) and the adenine group of ATP at the degenerate site may stimulate channel opening of poorly-phosphorylated human CFTR once the high-affinity Fe(iii) site at the interface of the regulatory (R) domain and ICL3 is removed.

scholarly journals Nucleotide-binding domain 1 of cystic fibrosis transmembrane conductance regulator

2000 ◽  
Vol 267 (17) ◽  
pp. 5306-5312 ◽  
Author(s):  
Francis Duffieux ◽  
Jean-Philippe Annereau ◽  
Julien Boucher ◽  
Emeric Miclet ◽  
Olivier Pamlard ◽  
...  
Keyword(s):  
Cystic Fibrosis ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Transmembrane Conductance Regulator ◽  
Nucleotide Binding Domain ◽  
Transmembrane Conductance ◽  
Cystic Fibrosis Transmembrane ◽  
Nucleotide Binding Domain 1
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