A novel model for the first nucleotide binding domain of the cystic fibrosis transmembrane conductance regulator

FEBS Letters

Stoven, Véronique²  Bontems, François²  Cuppens, Harry³  Cassiman, Jean-Jacques³  Tümmler, Burkhard¹  Annereau, Jean-Philippe²  Vankeerberghen, Anne³  Wulbrand, Ulrich¹ 

[1]Klinische Forschergruppe, Medizinische Hochschule, D-30623 Hannover, Germany

[2]Laboratoire de RMN, DCSO, Ecole Polytechnique, 91128 Palaiseau Cedex, France

[3]Center for Human Genetics, KU, Leuven, Belgium

关键词: Cystic fibrosis transmembrane conductance regulator;    Nucleotide binding fold;    Model building;    Cystic fibrosis;    Circular dichroism;    ABC transporter;   

DOI  :  10.1016/S0014-5793(97)00363-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 F₁-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.

【 授权许可】

Unknown