Structure and folding of potato type II proteinase inhibitors: Circular permutation and intramolecular domain swapping
Data(s) |
01/01/2005
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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 | |
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 |