Oxidative folding of the cystine knot motif in cyclotide proteins.
The cyclotides are a large family of plant proteins that have a cyclic backbone and a knotted arrangement of three conserved disulfide bonds. Despite the apparent complexity of their cystine knot motif it is possible to efficiently fold these proteins, as exemplified by oxidative folding studies on the prototypic cyclotide, kalata B1. This mini-review reports on the current understanding of the folding process in cyclotides. The synthesis and folding of these molecules paves the way for their application as stable molecular templates.
Craik
David J
DJ
Institute for Molecular Bioscience, University of Queensland, Brisbane, 4072, Australia. d.craik@imb.uq.edu.au
Daly
Norelle L
NL
D000595:Amino Acid Sequence; D000818:Animals; D047169:Cyclotides / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D047168:Cystine Knot Motifs; D004220:Disulfides / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D016415:Sequence Alignment
D047169:Cyclotides; D004220:Disulfides; D010940:Plant Proteins