Graduate School of Sciences, Information Technology and Engineering, CIAO, The University of Ballarat, MT Helen Campus, Victoria 3353, Australia.
Acta Biochim Biophys Sin (Shanghai). 2013 Jun;45(6):509-19. doi: 10.1093/abbs/gmt031. Epub 2013 Apr 5.
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 neurodegenerative diseases are caused by the conversion from a soluble normal cellular prion protein (PrP(C)) into insoluble abnormally folded infectious prions (PrP(Sc)). The hydrophobic region PrP(109-136) controls the formation of diseased prions: the normal PrP(113-120) 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-dimensional structures and structural dynamics.
朊病毒病，传统上被称为传染性海绵状脑病，是一种始终致命且高度感染的神经退行性疾病，影响着广泛的哺乳动物物种，在绵羊中表现为羊瘙痒病，在牛中表现为牛海绵状脑病（或“疯牛病”），在人类中表现为克雅氏病、格斯特曼-斯特劳斯勒-谢因克综合征、致命性家族性失眠症（FFI）和库鲁病等。这些神经退行性疾病是由可溶性正常细胞朊病毒蛋白（PrP(C))转化为不溶性异常折叠的传染性朊病毒（PrP(Sc))引起的。疏水区 PrP(109-136)控制着致病朊病毒的形成：正常的 PrP(113-120) AGAAAAGA 回文是朊病毒病的抑制剂/阻滞剂，高度保守的甘氨酸-xxx-甘氨酸基序 PrP(119-131)可以抑制感染性朊病毒蛋白在细胞中的形成。本文详细回顾了 PrP(109-136)区域，并介绍了其三维结构和结构动力学的研究。
