- Title
- Molecular dynamics studies on 3D structures of the hydrophobic region PrP(109-136)
- Creator
- Zhang, Jiapu; Zhang, Yuanli
- Date
- 2013
- Type
- Text; Journal article
- Identifier
- http://researchonline.federation.edu.au/vital/access/HandleResolver/1959.17/60661
- Identifier
- vital:5108
- Identifier
-
https://doi.org/10.1093/abbs/gmt031
- Identifier
- ISSN:1672-9145
- Abstract
- 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 'madcow' 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. © The Author 2013.
- Relation
- Acta Biochimica et Biophysica Sinica Vol. 45, no. 6 (2013), p. 509-519
- Rights
- Copyright 2013 The Authors
- Rights
- Open Access
- Rights
- This metadata is freely available under a CCO license
- Subject
- 0601 Biochemistry and Cell Biology; AGAA AAGA palindrome; Glycine-xxx-glycine motif; Hydrophobic region; Molecular dynamics study; PrP(109-136)
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