ニュース

2018年02月07日 掲載 (Published 02/07/2018)


「Biophysics and Physicobiology」にMitsuhiko Odera et al. “Molecular dynamics simulation study on the structural instability of the most common cystic fibrosis-associated mutant ΔF508-CFTR” を掲載

日本生物物理学会欧文誌[Biophysics and Physicobiology]に以下の論文が新規掲載されました。

Mitsuhiko Odera, Tadaomi Furuta, Yoshiro Sohma and Minoru Sakurai
“Molecular dynamics simulation study on the structural instability of the most common cystic fibrosis-associated mutant ΔF508-CFTR”

【Significance】
ΔF508 CFTR

CFTR is an anion channel that belongs to the ABC transporter superfamily. Deletion of F508 (ΔF508) is known to cause serious gating defects. Our MD simulations revealed two posible origins of the functional defects of this mutant. First, the deletion of F508 causes a disruption of a hydrophobic cluster located at the interface between the nucleotide binding domain 1 (NBD1) and intracellular loop 4. Second, the effect of the F508 deletion propagates into the NBD1–NBD2 interface, resulting in the impairment of their correct dimerization. These findings are useful for drug design.


Biophysics and Physicobiology, Vol.15, pp. 33-44

URL:https://www.jstage.jst.go.jp/article/biophysico/15/0/15_33/_article