1r1f
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(New page: 200px<br /><applet load="1r1f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r1f" /> '''Solution Structure of the Cyclotide Palicour...)
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Revision as of 23:04, 20 November 2007
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Solution Structure of the Cyclotide Palicourein: Implications for the development of pharmaceutical and agricultural applications
Overview
The cyclotides are a family of disulfide-rich proteins from plants. They, have the characteristic structural features of a circular protein backbone, and a knotted arrangement of disulfide bonds. Structural and biochemical, studies of the cyclotides suggest that their unique physiological, stability can be loaned to bioactive peptide fragments for pharmaceutical, and agricultural development. In particular, the cyclotides incorporate a, number of solvent-exposed loops that are potentially suitable for epitope, grafting applications. Here, we determine the structure of the largest, known cyclotide, palicourein, which has an atypical size and composition, within one of the surface-exposed loops. The structural data show that an, increase in size of a palicourein loop does not perturb the core fold, to, which the thermodynamic and chemical stability has been attributed. The, cyclotide core fold, thus, can in principle be used as a framework for the, development of useful pharmaceutical and agricultural bioactivities.
About this Structure
1R1F is a Single protein structure of sequence from Palicourea condensata. Full crystallographic information is available from OCA.
Reference
Solution structure of the cyclotide palicourein: implications for the development of a pharmaceutical framework., Barry DG, Daly NL, Bokesch HR, Gustafson KR, Craik DJ, Structure. 2004 Jan;12(1):85-94. PMID:14725768
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