In vivo crystals reveal critical features of the interaction between cystic fibrosis transmembrane conductance regulator (CFTR) and the PDZ2 domain of Na(+)/H(+) exchange cofactor NHERF1.
in addition to its role in Cl- transport HI-NBD2 domain confers membrane stability of CFTR by consolidating its quaternary structure through interactions with HI-NBD1 region.
analysis of domain location within the cystic fibrosis transmembrane conductance regulator protein investigated by electron microscopy and gold labelling
results directly link ATP-driven tight dimerization of CFTR's cytoplasmic nucleotide-binding domains to opening of the ion channel in the transmembrane domains; ATP-driven tight dimerization of CFTR's cytoplasmic nucleotide-binding domains is linked to opening of the ion channel suggesting that CFTR employs a molecular mechanism similar to that used by other ABC transporters.
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