1yp8
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of the cyclotide tricyclon A
OverviewOverview
Cyclotides are a family of plant proteins that have the unusual combination of head-to-tail backbone cyclization and a cystine knot motif. They are exceptionally stable and show resistance to most chemical, physical, and enzymatic treatments. The structure of tricyclon A, a previously unreported cyclotide, is described here. In this structure, a loop that is disordered in other cyclotides forms a beta sheet that protrudes from the globular core. This study indicates that the cyclotide fold is amenable to the introduction of a range of structural elements without affecting the cystine knot core of the protein, which is essential for the stability of the cyclotides. Tricyclon A does not possess a hydrophobic patch, typical of other cyclotides, and has minimal hemolytic activity, making it suitable for pharmaceutical applications. The 22 kDa precursor protein of tricyclon A was identified and provides clues to the processing of these fascinating miniproteins.
About this StructureAbout this Structure
1YP8 is a Protein complex structure of sequences from Viola tricolor. Full crystallographic information is available from OCA.
ReferenceReference
Processing of a 22 kDa precursor protein to produce the circular protein tricyclon A., Mulvenna JP, Sando L, Craik DJ, Structure. 2005 May;13(5):691-701. PMID:15893660
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