Molecular Dynamics Studies on 3D Structures of the Hydrophobic Region PrP(109-136)

TL;DR

This paper reviews the 3D structures and dynamics of the hydrophobic region 109-136 in prion proteins, elucidating its role in prion disease conversion and progression.

Contribution

It provides detailed structural and dynamic analyses of the 109-136 region, highlighting its significance in prion disease mechanisms.

Findings

Structural insights into the 109-136 region

Dynamics related to prion conversion

Potential targets for therapeutic intervention

Abstract

Prion diseases caused by the conversion from a soluble normal cellular prion protein into insoluble abnormally folded infectious prions, are invariably fatal and highly infectious degenerative diseases that affect a wide variety of mammalian species. The palindrome and the Glycine-rich conserved segment in the hydrophobic region 109-136 control the conversion from normal prion protein to form into diseased prions. This paper gives detailed reviews on the 109-136 region and presents the studies of its 3D structures and structural dynamics.