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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 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 (PrPC) into insoluble abnormally folded infectious prions (PrPSc). 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.

Authors:   Jiapu Zhang; Yuanli Zhang
Journal:   Acta Biochimica et Biophysica Sinica
Volume:   45
edition:   6
Year:   2013
Pages:   509
DOI:   10.1093/abbs/gmt031
Publication date:   01-Jun-2013
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