| Primary Identifier | IPR008176 | Type | Family |
| Short Name | Defensin_plant |
| 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 β-sheet and a short α-helix []. Three disulphide bridges are located in the hydrophobic core between the helix and sheet, forming a cysteine-stabilised α-helical motif. This structure differs from that of the plant alpha- and beta- thionins, but is analogous to scorpion toxins and insect defensins. |
