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Molecular Structures and Structural Dynamics of Prion Proteins and Prions pp 143–166Cite as

The Hydrophobic Region PrP(109–136)

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Part of the book series: Focus on Structural Biology ((FOSB,volume 9))

Abstract

Prion diseases , traditionally referred to as TSE, are invariably fatal and highly infectious neurodegenerative diseases that affect a wide variety of mammalian species, manifesting as scrapie in sheep, BSE or ‘mad-cow’ disease in cattle, and CJD, GSS, 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 into diseased prions: the normal PrP(113–120) AGAAAAGA palindrome is an inhibitor/blocker of prion diseases (Mol Cell Neurosci 15:66–78), and the highly conserved Glycine-xxx-Glycine motif PrP(119–131) can inhibit the formation of infectious prion proteins in cells (J Biol Chem 285:20213–20223). This chapter presents the studies of the 3D structures and structural dynamics of PrP(109–136).

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  1. School of Sciences Information Technology and Engineering, The Federation University, Ballarat, VIC, Australia

    Jiapu Zhang

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Zhang, J. (2015). The Hydrophobic Region PrP(109–136). In: Molecular Structures and Structural Dynamics of Prion Proteins and Prions. Focus on Structural Biology, vol 9. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-7318-8_10

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