Structural highlights
Publication Abstract from PubMed
Two polypeptides named vodo M and vodo N, both of 29 amino acids, have been isolated from Viola odorata L. (Violaceae) using ion exchange chromatography and reversed phase HPLC. The sequences were determined by automated Edman degradation, quantitative amino acid analysis, and mass spectrometry (MS). Using MS, it was established that vodo M (cyclo-SWPVCTRNGAPICGESCFTGKCYTVQCSC) and vodo N (cyclo-SWPVCYRNGLPVCGETCTLGKCYTAGCSC) form a head-to-tail cyclic backbone and that six cysteine residues are involved in three disulphide bonds. Their origin, sequences, and cyclic nature suggest that these peptides belong to the family of cyclic plant peptides, called cyclotides. The three-dimensional structures of vodo M and vodo N were modelled by homology, using the experimentally determined structure of the cyclotide kalata B1 as the template. The images of vodo M and vodo N show amphipathic structures with considerable surface hydrophobicity for a protein modelled in a polar environment.
Primary and 3-D modelled structures of two cyclotides from Viola odorata.,Svangard E, Goransson U, Smith D, Verma C, Backlund A, Bohlin L, Claeson P Phytochemistry. 2003 Sep;64(1):135-42. PMID:12946412[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Svangard E, Goransson U, Smith D, Verma C, Backlund A, Bohlin L, Claeson P. Primary and 3-D modelled structures of two cyclotides from Viola odorata. Phytochemistry. 2003 Sep;64(1):135-42. PMID:12946412
