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

作　　者：Jiapu Zhang Yuanli Zhang 

机构地区：[1]Graduate School of Sciences, Information Technology and Engineering, CIAO, The University of Ballarat, MT Helen Campus,Victoria 3353, Australia [2]School of Basic Medical Sciences, Taishan Medical University, Tai'an 271000, China

出　　处：《Acta Biochimica et Biophysica Sinica》2013年第6期509-519,共11页生物化学与生物物理学报（英文版）

摘　　要：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.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.

关 键 词：hydrophobic region PrP（109-136） AGAAAAGA palindrome glycine-xxx-glycine motif moleculardynamics study 

分 类 号：S858.237.1[农业科学—临床兽医学] TB383[农业科学—兽医学]