1yp8
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(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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Revision as of 04:50, 21 November 2007
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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 Wed Nov 21 06:57:46 2007
