Structure and folding of potato type II proteinase inhibitors: circular permutation and intramolecular domain swapping

Protein Pept Lett. 2005 Jul;12(5):421-31. doi: 10.2174/0929866054395266.

Abstract

Potato type II serine proteinase inhibitors are proteins that consist of multiple sequence repeats, and exhibit a multidomain structure. The structural domains are circular permutations of the repeat sequence, as a result of intramolecular domain swapping. Structural studies give indications for the origins of this folding behaviour, and the evolution of the inhibitor family.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Evolution, Molecular
  • Plant Proteins
  • Protease Inhibitors / chemistry*
  • Protease Inhibitors / metabolism*
  • Protein Folding*
  • Solanaceae / enzymology
  • Structure-Activity Relationship

Substances

  • Plant Proteins
  • Protease Inhibitors
  • potato proteinase inhibitor II-b