期刊
PRION
卷 4, 期 1, 页码 38-44出版社
TAYLOR & FRANCIS INC
DOI: 10.4161/pri.4.1.10890
关键词
prion; Creutzfeldt-Jakob disease; fragment molecular orbital calculation; molecular interaction; structural stability
资金
- Ministry of Agriculture, Forestry and Fisheries Research Network (MAFFIN)
- BSE
- Ministry of Agriculture, Forestry and Fisheries, Japan
The E200K mutation of the human prion protein (PrP) is known to cause familial Creutzfeldt-Jakob disease. In order to elucidate the effects of the mutation on the local structural stability of PrP, we performed ab initio fragment molecular orbital calculations for the wild-type human PrP and the E200K variant modeled under neutral and mild acidic conditions. The calculations revealed that this substitution markedly altered the intramolecular interactions in the PrP, suggesting that the local structural instabilities induced by the E200K mutation might cause initial denaturation of the PrP and its subsequent conversion to a pathogenic form. This work presents a new approach for quantitatively elucidating structural instabilities in proteins that cause misfolding diseases.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据