Molecular dynamics studies on 3D structures of the hydrophobic region PrP（109-136）

Prion diseases, traditionally referred to as transmissible spongiform encephalopathies, are invariably fatal and highly infectious neurodegenerative diseases that affect a wide variety of mammalian species, manifesting as scrapie in sheep, bovine spongiform encephalopathy （or ＇mad- cow＇ disease） in...

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Published in生物化学与生物物理学报：英文版 no. 6; pp. 509 - 519
Main Author Jiapu Zhang Yuanli Zhang
Format Journal Article
LanguageEnglish
Published 2013
Subjects
PrP
三维结构
传染性海绵状脑病
分子动力学
朊病毒疾病
牛海绵状脑病
疏水
神经退行性疾病
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Summary:Prion diseases, traditionally referred to as transmissible spongiform encephalopathies, are invariably fatal and highly infectious neurodegenerative diseases that affect a wide variety of mammalian species, manifesting as scrapie in sheep, bovine spongiform encephalopathy （or ＇mad- cow＇ disease） in cattle, and Creutzfeldt-Jakob disease, Gerstmann-Strussler-Scheinker syndrome, fatal familial insomnia （FFI）, and Kulu in humans, etc. These neurode- generative diseases are caused by the conversion from a soluble normal cellular prion protein （PrPc） into insoluble abnormally folded infectious prions （prpSC）. The hydro- phobic region PrP（109-136） controls the formation of dis- eased prions： the normal PrP（ll3-120） AGAAAAGA palindrome is an inhibitor/blocker of prion diseases and the highly conserved glycine-xxx-glycine motif PrP（119- 131） can inhibit the formation of infectious prion proteins in cells. This article gives detailed reviews on the PrP（109- 136） region and presents the studies of its three-dimen- sional structures and structural dynamics.
Bibliography:31-1940/Q
Prion diseases, traditionally referred to as transmissible spongiform encephalopathies, are invariably fatal and highly infectious neurodegenerative diseases that affect a wide variety of mammalian species, manifesting as scrapie in sheep, bovine spongiform encephalopathy （or ＇mad- cow＇ disease） in cattle, and Creutzfeldt-Jakob disease, Gerstmann-Strussler-Scheinker syndrome, fatal familial insomnia （FFI）, and Kulu in humans, etc. These neurode- generative diseases are caused by the conversion from a soluble normal cellular prion protein （PrPc） into insoluble abnormally folded infectious prions （prpSC）. The hydro- phobic region PrP（109-136） controls the formation of dis- eased prions： the normal PrP（ll3-120） AGAAAAGA palindrome is an inhibitor/blocker of prion diseases and the highly conserved glycine-xxx-glycine motif PrP（119- 131） can inhibit the formation of infectious prion proteins in cells. This article gives detailed reviews on the PrP（109- 136） region and presents the studies of its three-dimen- sional structures and structural dynamics.
hydrophobic region; PrP（109-136）; AGAAAAGA palindrome; glycine-xxx-glycine motif; moleculardynamics study
ISSN:1672-9145
1745-7270