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''' | '''Solution structure of the cyclotide tricyclon A''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | 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://www.ncbi.nlm.nih.gov/pubmed/15893660 15893660] | 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: Viola tricolor]] | ||
[[Category: Craik, D J.]] | [[Category: Craik, D J.]] | ||
[[Category: Mulvenna, J P.]] | [[Category: Mulvenna, J P.]] | ||
[[Category: Sando, L.]] | [[Category: Sando, L.]] | ||
| - | [[Category: | + | [[Category: Beta-sheet]] |
| - | [[Category: | + | [[Category: Cyclic backbone]] |
| - | [[Category: | + | [[Category: Cyclotide]] |
| - | [[Category: | + | [[Category: Cystine knot]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:36:37 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 13:36, 3 May 2008
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
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 Sat May 3 16:36:37 2008
