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