| Type: | Family | Name: | Gamma-thionin |
| Description: | The following small plant proteins are evolutionary related:Gamma-thionins from Triticum aestivum(Wheat) endosperm (gamma-purothionins) and gamma-hordothionins from Hordeum vulgare(Barley) are toxic to animal cells and inhibit protein synthesis in cell free systems [].A flower-specific thionin (FST) from Nicotiana tabacum(Common Tobacco)[].Antifungal proteins (AFP) from the seeds of Brassicaceae species such as radish, mustard, turnip and Arabidopsis thaliana(Thale Cress)[].Inhibitors of insect alpha-amylases from sorghum [].Probable protease inhibitor P322 from Solanum tuberosum(Potato).A germination-related protein from Vigna unguiculata(Cowpea) [].Anther-specific protein SF18 from sunflower. SF18 is a protein that contains a gamma-thionin domain at its N terminus and a proline-rich C-terminal domain.Glycine max(Soybean) sulphur-rich protein SE60 [].Vicia faba(Broad bean) antibacterial peptides fabatin-1 and -2.In their mature form, these proteins generally consist of about 45 to 50 amino-acid residues. As shown in the following schematic representation, these peptides contain eight conserved cysteines involved in disulphide bonds.+-------------------------------------------+ | +-------------------+ || | | | xxCxxxxxxxxxxCxxxxxCxxxCxxxxxxxxxCxxxxxxCxCxxxC| | | | +---|----------------+ |+------------------+ 'C': conserved cysteine involved in a disulphide bond.The folded structure of Gamma-purothionin is characterised by a well-defined 3-stranded anti-parallel beta-sheet and a short alpha-helix []. Three disulphide bridges are located in the hydrophobic core between the helix and sheet, forming a cysteine-stabilised alpha-helical motif. This structure differs from that of the plant alpha- and beta- thionins, but is analogous to scorpion toxins and insect defensins. | Short Name: | Gamma-thionin |
