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首页> 外文期刊>Biochemistry >Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation.
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Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation.

机译：囊性纤维化跨膜电导调节剂：基于Phe508区的肽的溶液结构，Phe508区是引起疾病的DeltaF508突变的最常见部位。

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摘要

Most cases of cystic fibrosis (CF), a common inherited disease of epithelial cell origin, are caused by the deletion of Phe508 located in the first nucleotide-binding domain (NBF1) of the protein called CFTR (cystic fibrosis transmembrane conductance regulator). To gain greater insight into the structure within the Phe508 region of the wild-type protein and the change in structure that occurs when this residue is deleted, we conducted nuclear magnetic resonance (NMR) studies on representative synthetic 26 and 25 amino acid peptide segments. 2D 1H NMR studies at 600 MHz of the 26-residue peptide consisting of Met498 to Ala523 in 10% DMSO, pH 4.0, at 25 degrees C show a continuous but labile helix from Gly500 to Lys522, based on both NH-NH(i,i+1) and alphaH-NH(i,i+1) NOEs. Phe508 within this helix shows only short-range (i,
机译：囊性纤维化（CF）的大多数情况是上皮细胞起源的常见遗传疾病，是由位于称为CFTR（囊性纤维化跨膜电导调节剂）的蛋白质的第一个核苷酸结合域（NBF1）中的Phe508缺失引起的。为了更深入地了解野生型蛋白Phe508区域内的结构以及删除该残基时发生的结构变化，我们对代表性的26和25个氨基酸合成肽段进行了核磁共振（NMR）研究。由25％的10％DMSO（pH 4.0）中的Met498到Ala523组成的26个残基的肽在25摄氏度下于600 MHz的2D 1H NMR研究表明，从NH-NH（i， i + 1）和alphaH-NH（i，i + 1）NOE。此螺旋中的Phe508仅显示短距离（i，

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