1yp8
From Proteopedia
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| - | [[Image:1yp8.gif|left|200px]] | + | [[Image:1yp8.gif|left|200px]] |
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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= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Solution structure of the cyclotide tricyclon A''' | ||
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==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 13:25, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of the cyclotide tricyclon A
Overview
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 Structure
1YP8 is a Protein complex structure of sequences from Viola tricolor. Full crystallographic information is available from OCA.
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:15893660
Page seeded by OCA on Thu Mar 20 15:25:46 2008
