Structure and folding of potato type II proteinase inhibitors: circular permutation and intramolecular domain swapping.
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.
Schirra
Horst Joachim
HJ
Institute for Molecular Bioscience, University of Queensland. Brisbane, Qld 4072, Australia.
Craik
David J
DJ
D019143:Evolution, Molecular; D010940:Plant Proteins; D011480:Protease Inhibitors / Q000737:chemistry* / Q000378:metabolism*; D017510:Protein Folding; D019657:Solanaceae / Q000201:enzymology; D013329:Structure-Activity Relationship
D010940:Plant Proteins; D011480:Protease Inhibitors; C009011:potato proteinase inhibitor II-b