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Prion protein: evolution caught en route.

P Tompa1, G E Tusnády, M Cserzo

  • 1Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, P.O. Box 7, H-1518 Budapest, Hungary.

Proceedings of the National Academy of Sciences of the United States of America
|April 5, 2001
PubMed
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The prion protein

Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Structural Biology

Background:

  • The prion protein (PrP) exhibits structural ambiguity, adopting multiple stable conformations.
  • This ambiguity is puzzling under physiological conditions.

Purpose of the Study:

  • To investigate the evolutionary and structural basis for prion protein's conformational flexibility.
  • To propose a hypothesis for PrP's structural evolution based on its environmental shift.

Main Methods:

  • Analysis of known vertebrate prion protein sequences.
  • Comparative sequence analysis to identify ancestral protein features.

Main Results:

  • Evidence suggests a primordial transmembrane protein is encrypted within vertebrate prion sequences.

Related Experiment Videos

  • This indicates a past relocalization event where PrP moved from a membrane to the extracellular space.
  • The evolutionary timeframe may have been insufficient for PrP to achieve a fully stable, "minimally frustrated" globular structure.

    • Conclusions:

    • The prion protein's structural ambiguity stems from its evolutionary transition from an integral membrane protein to an extracellular one.
    • Functional constraints related to flexibility may have hindered the development of a stable globular fold.
    • Prion protein's structure is still evolving towards a more defined globular state.