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

作者：Zhang Jiapu^*; Zhang Yuanli

来源：Acta Biochimica et Biophysica Sinica, 2013, 45(6): 509-519.

DOI：10.1093/abbs/gmt031

• hydrophobic region
• PrP(109-136)
• AGAAAAGA palindrome
• glycine-xxx-glycine motif
• molecular dynamics study

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 CreutzfeldtJakob disease, GerstmannStrusslerScheinker 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.

• 出版日期2013-6
• 单位山东第一医科大学