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A novel model for the first nucleotide binding domain of the cystic fibrosis transmembrane conductance regulator
Author(s) -
Annereau Jean-Philippe,
Wulbrand Ulrich,
Vankeerberghen Anne,
Cuppens Harry,
Bontems François,
Tümmler Burkhard,
Cassiman Jean-Jacques,
Stoven Véronique
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00363-3
Subject(s) - cystic fibrosis transmembrane conductance regulator , cyclic nucleotide binding domain , cystic fibrosis , regulator , mutation , δf508 , nucleotide , transmembrane domain , transmembrane protein , biology , microbiology and biotechnology , chemistry , gene , biophysics , genetics , receptor
Cystic fibrosis is caused by mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) gene. The most frequent mutation is the deletion of F508 in the first nucleotide binding fold (NBF1). It induces a perturbation in the folding of NBF1, which impedes posttranslational maturation of CFTR. Determination of the three‐dimensional structure of NBF1 would help to understand this defect. We present a novel model for NBF1 built from the crystal structure of bovine mitochondrial F 1 ‐ATPase protein. This model gives a reasonable interpretation of the effect of mutations on the maturation of the protein and, in agreement with the CD data, leads to reconsideration of the limits of NBF1 within CFTR.