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Article

The CFTR P67L variant reveals a key role for N-terminal lasso helices in channel folding, maturation, and pharmacologic rescue.

The Journal of biological chemistry - 1 Jan 2000

Sabusap Carleen Mae, Joshi Disha, Simhaev Luba, Oliver Kathryn E, Senderowitz Hanoch, van Willigen Marcel, Braakman Ineke, Rab Andras, Sorscher Eric J, Hong Jeong S

Abstract excerpt

Patients with cystic fibrosis (CF) harboring the P67L variant in the cystic fibrosis transmembrane conductance regulator (CFTR) often exhibit a typical CF phenotype, including severe respiratory compromise. This rare mutation (reported in <300 patients worldwide) responds robustly to CFTR correctors, such as lumacaftor and tezacaftor, with rescue in model systems that far exceed what can be achieved for the...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 33781744
DOI: 10.1016/j.jbc.2021.100598
PMCID: PMC8102917

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