Structure-function aspects of prion proteins

Curr Opin Biotechnol. 1998 Aug;9(4):359-65. doi: 10.1016/s0958-1669(98)80008-6.

Abstract

Prions diseases are fatal neurodegenerative disorders resulting from conformational changes in the prion protein from the normal cellular form, PrPC, to the infectious scrapie isoform, PrPSc. High resolution structures for PrPC are now available, and biochemical investigations are shedding light on the nature and determinants of the conformational transition. Together, these studies are beginning to provide a framework to describe structure-function relationships of the prion protein.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Humans
  • Magnetic Resonance Spectroscopy
  • PrPC Proteins / chemistry
  • PrPC Proteins / metabolism*
  • PrPSc Proteins / chemistry
  • PrPSc Proteins / metabolism
  • Prions / chemistry*
  • Prions / physiology*
  • Protein Conformation
  • Species Specificity
  • Structure-Activity Relationship

Substances

  • PrPC Proteins
  • PrPSc Proteins
  • Prions