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

• Published in: Acta biochimica et biophysica Sinica Vol. 45; no. 6; pp. 509 - 519
• Main Authors: Zhang, Jiapu, Zhang, Yuanli
• Format: Journal Article
• Language: English
• Published: China 01.06.2013
• Subjects: Amino Acid Sequence; Animals; Humans; Hydrophobic and Hydrophilic Interactions; Molecular Dynamics Simulation; Molecular Sequence Data; Prions - chemistry; Protein Conformation; Sequence Homology, Amino Acid; PrP(109-136); AGAAAAGA palindrome; molecular dynamics study; glycine-xxx-glycine motif; hydrophobic region
• ISSN: 1672-9145; 1745-7270
• DOI: 10.1093/abbs/gmt031

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.