1yp8
From Proteopedia
(New page: 200px<br /><applet load="1yp8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yp8" /> '''Solution structure of the cyclotide tricyclo...) |
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| - | [[Image:1yp8.gif|left|200px]]<br /><applet load="1yp8" size=" | + | [[Image:1yp8.gif|left|200px]]<br /><applet load="1yp8" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''Solution structure of the cyclotide tricyclon A'''<br /> | '''Solution structure of the cyclotide tricyclon A'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cyclotides are a family of plant proteins that have the unusual | + | 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== | ==About this Structure== | ||
| - | 1YP8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Viola_tricolor Viola tricolor]. Full crystallographic information is available from [http:// | + | 1YP8 is a [http://en.wikipedia.org/wiki/Protein_complex 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== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Viola tricolor]] | [[Category: Viola tricolor]] | ||
| - | [[Category: Craik, D | + | [[Category: Craik, D J.]] |
| - | [[Category: Mulvenna, J | + | [[Category: Mulvenna, J P.]] |
[[Category: Sando, L.]] | [[Category: Sando, L.]] | ||
[[Category: beta-sheet]] | [[Category: beta-sheet]] | ||
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[[Category: cystine knot]] | [[Category: cystine knot]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:07:39 2008'' |
Revision as of 14:07, 21 February 2008
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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 Feb 21 16:07:39 2008
