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


Autoria(s): Schirra, H. J.; Craik, D. J.
Data(s)

01/01/2005

Resumo

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 or intramolecular domain swapping. Structural studies give indications for the origins of this folding behaviour, and the evolution of the inhibitor family.

Identificador

http://espace.library.uq.edu.au/view/UQ:75818

Idioma(s)

eng

Publicador

Bentham Science Publ Ltd

Palavras-Chave #Proteinase Inhibitors #Potato Type 2 Inhibitors #Circular Permutation #Domain Swapping #Protein Folding #Protein Structure #Biochemistry & Molecular Biology #X-ray-analysis #Nicotiana-alata #Concanavalin-a #Precursor Protein #3-dimensional Structure #Sunflower Seeds #Eye Lens #Resolution #Sequence #Plants #C1 #250302 Biological and Medical Chemistry #780105 Biological sciences
Tipo

Journal Article