Prion Protein Misfolding and Disease

Overview

Journal Curr Opin Struct Biol

Date 2009 Jan 23

PMID 19157856

Citations 36

Authors

Roger A Moore

Lara M Taubner

Suzette A Priola

Affiliations

Soon will be listed here.

Abstract

Transmissible spongiform encephalopathies (TSEs or prion diseases) are a rare group of invariably fatal neurodegenerative disorders that affect humans and other mammals. TSEs are protein misfolding diseases that involve the accumulation of an abnormally aggregated form of the normal host prion protein (PrP). They are unique among protein misfolding disorders in that they are transmissible and have different strains of infectious agents that are associated with unique phenotypes in vivo. A wealth of biological and biophysical evidence now suggests that the molecular basis for prion diseases may be encoded by protein conformation. The purpose of this review is to provide an overview of the existing structural information for PrP within the context of what is known about the biology of prion disease.

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