Loss of function of the CFTR anion channel leads to cystic fibrosis, the most common inherited condition in humans of European origin. A recently reported structure for CFTR at 3.7-Å resolution reveals an unexpected 'lasso' domain and provides new insights into channel function in healthy individuals and in people with cystic fibrosis.
References
Riordan, J.R. et al. Science 245, 1066–1073 (1989).
Van Goor, F. et al. Proc. Natl. Acad. Sci. USA 106, 18825–18830 (2009).
Zhang, Z. & Chen, J. Cell 167, 1586–1597 (2016).
Bozoky, Z. et al. Proc. Natl. Acad. Sci. USA 110, E4427–E4436 (2013).
Aleksandrov, A.A. et al. J. Mol. Biol. 419, 41–60 (2012).
Gee, H.Y., Tang, B.L., Kim, K.H. & Lee, M.G. J. Biol. Chem. 285, 35519–35527 (2010).
Eckford, P.D., Li, C., Ramjeesingh, M. & Bear, C.E. J. Biol. Chem. 287, 36639–36649 (2012).
Sheppard, D.N. & Welsh, M.J. Physiol. Rev. 79, S23–S45 (1999).
Van Goor, F. et al. Pediatr. Pulmonol. 44, 154–155 (2009).
Author information
Authors and Affiliations
Corresponding author
Ethics declarations
Competing interests
B.F. consulted in 2015 and 2016 for Vertex, Inc., which discovered and currently markets ivacaftor.
Rights and permissions
About this article
Cite this article
Ford, B. CFTR structure: lassoing cystic fibrosis. Nat Struct Mol Biol 24, 13–14 (2017). https://doi.org/10.1038/nsmb.3353
Published:
Issue Date:
DOI: https://doi.org/10.1038/nsmb.3353
- Springer Nature America, Inc.