Abstract:
The castor bean (Ricinus communis L.) belongs to the euphorbiaceae family and is native to Africa. This plant is an agro-economical bean that grows in warm climate. Ricin toxin (RT) is extracted from seed of castor bean (R. communis) plant which is type II ribosome-inactivating protein (RIP). Ricin, a cytotoxin is a heterodimer that consists of a surface that bind cell with ricin B chain (RTB) and ricin A chain (RTA) with enzyme N-glycosidase. This study was aimed to identify the intrinsic disordered region in different amino acids of ricin protein through 3D-structure formation, quality assessment and refinement. The 3D structure of ricin was determined by in-silico various tools like SWISS-model and Phyre 2. The templates that were used to generate the 3-D model were based on similarity scores and amino acid distribution. This research work has demonstrated the phylogenetic tree complexity of amino acids sequence in ricin protein that was analyzed by study with related other plants through multiple alignment sequence. Intrinsically disordered regions of ricin were predicted by PONDER, IUPred, MfDp tool that showed the quality of disorder in amino acids regions included short, long, and all terminal areas (C and N). These representations showed result in graphical form, specifying the tendency of toxic residues in ricin sequence The quality assessment and refinement of structure was performed using computational tools like ProSA-web, Verify 3D, ERRAT. The refined ricin monomer structure was used to identify transformation data that was generated in the form of numerous homo-trimmer solutions. The Chimmera and Protter tools were used to visualized 3D structure of ricin and displayed that the extracellular query protein has signal peptide ranged from 1035 amino acids alignment of sequence in multi align viewer. Homology modeling 3D- structure of template sequence identity and coverage was 100% with ricin a chain that showed total diffraction 2.60 Å in SWISS-model. The results showed the highest disorder tendency graphs, the interactive visualization and refinement of the ricin protein. In anticipated research work has revealed that toxic region in amino acids of ricin protein was predicted through different in-silico approaches. By knowing the determined ordered and disordered region in ricin further studies about reducing the toxicity of ricin would be helpful and faster.
Page(s):
18-18
DOI:
DOI not available
Published:
Journal: Abstract Book on Second International Conference on Recent Approaches in Plant Sciences (RAPS-23) 4-5 May 2023 , Volume: 0, Issue: 0, Year: 2023