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Univ. of Texas SW Medical Center, Dallas

CFTR folding analyzed, contributions of side chain and backbone revealed

Published in Physician Law Weekly, March 23rd, 2005

Investigators from the United States have documented side chain and backbone contributions of Phe508 to cystic fibrosis transmembrane conductance regulator (CFTR) folding.

"Mutations in the CFTR, an integral membrane protein, cause cystic fibrosis (CF). The most common CF-causing mutant, deletion of Phe508, fails to properly fold. To elucidate the role Phe508 plays in the folding of CFTR, missense mutations at this position were generated," wrote P.H. Thibodeau and colleagues, University of Texas Southwestern Medical Center.

"Only one missense mutation had a pronounced effect on the stability and folding of the isolated domain in vitro. In contrast,...

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