1yp8

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yp8 OCA], [http://www.ebi.ac.uk/pdbsum/1yp8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yp8 RCSB]</span>
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[[Category: cystine knot]]
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Revision as of 22:16, 30 March 2008


PDB ID 1yp8

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Resources: FirstGlance, OCA, PDBsum, RCSB
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

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