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Biochem Biophys Res Commun. 2017 Sep 30;491(4):986-993. doi: 10.1016/j.bbrc.2017.07.165. Epub 2017 Jul 31.

Molecular dynamics of the cryo-EM CFTR structure.

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Department of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary.
Department of Applied Biotechnology and Food Science, Budapest University of Technology and Economics, Budapest, Hungary; Genome Metabolism Group, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Hungary.
Department of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary; Membrane Research Group, Hungarian Academy of Sciences, Budapest, Hungary. Electronic address:


Cystic fibrosis (CF), a lethal monogenic disease, is caused by mutant variants of the CF transmembrane conductance regulator (CFTR). Recent advances in single molecule cryo-EM methods enabled structural determination of full-length human and zebrafish CFTR, achieving an important milestone for CF drug development. To relate these structures to the gating cycle, we examined its dynamic features using molecular dynamics simulations. Our results show that the nucleotide binding domains (NBDs) in this bottom-open apo conformation exhibit motions related to dimerization and the bottom-closed apo CFTR model indicates opening of NBDs in contrast to transporters. These observations help in understanding the properties of CFTR chloride channel distinct from transporters and in proper interpretation of available structural information on this ABC protein.


CFTR; Computational biology; Cystic fibrosis; Molecular dynamics; Transmembrane protein structure

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