Structure and Folding of Potato Type II Proteinase Inhibitors: Circular Permutation and Intramolecular Domain Swapping

Title: Structure and Folding of Potato Type II Proteinase Inhibitors: Circular Permutation and Intramolecular Domain Swapping

Volume: 12 Issue: 5

Author(s): Horst Joachim Schirra and David J. Craik

Affiliation:

Keywords: proteinase inhibitors, potato type inhibitors, circular permutation, domain swapping, protein folding, protein structure

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.

Cite this article as:

Schirra Joachim Horst and Craik J. David, Structure and Folding of Potato Type II Proteinase Inhibitors: Circular Permutation and Intramolecular Domain Swapping, Protein & Peptide Letters 2005; 12 (5) . https://dx.doi.org/10.2174/0929866054395266