1yp8: Difference between revisions
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'''Solution structure of the cyclotide tricyclon A''' | {{Structure | ||
|PDB= 1yp8 |SIZE=350|CAPTION= <scene name='initialview01'>1yp8</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
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'''Solution structure of the cyclotide tricyclon A''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1YP8 is a [ | 1YP8 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Viola_tricolor Viola tricolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YP8 OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15893660 15893660] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Viola tricolor]] | [[Category: Viola tricolor]] | ||
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[[Category: cystine knot]] | [[Category: cystine knot]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:25:46 2008'' | ||
Revision as of 16:25, 20 March 2008
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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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