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The prion folding problem

P M Harrison1, P Bamborough, V Daggett

  • 1University of California, Box Number 450, San Francisco, CA-94143, USA.

Current Opinion in Structural Biology
|February 1, 1997
PubMed
Summary
This summary is machine-generated.

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Prion diseases involve structural changes in prion proteins, shifting from alpha-helical to beta-sheet structures. This unique mechanism underlies these neurodegenerative disorders.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Structural Biology

Background:

  • Prion diseases are fatal neurodegenerative conditions.
  • The central event is a conformational change in the prion protein (PrP).
  • This involves a loss of alpha-helical and gain of beta-sheet content.

Purpose of the Study:

  • To investigate the unprecedented mechanism of prion diseases.
  • To understand the structural transition of the prion protein.

Main Methods:

  • Review of recent biological studies.
  • Analysis of structural biology data.

Main Results:

  • Prion protein structural transition is fundamental to disease.
  • The conformational change involves loss of alpha-helical and gain of beta-sheet structure.

Related Experiment Videos

  • Evidence suggests a truly unprecedented disease mechanism.

    • Conclusions:

    • The mechanism underlying prion diseases is unique.
    • Understanding this mechanism is key to addressing these neurodegenerative disorders.