In silico structural and interactional study of wheat proteins gliadin and glutenin with comparison to wheat toxin alpha-purothionin
1 Gomal Centre of Biochemistry and Biotechnology, Gomal University, Dera Ismail Khan 29050, Khyber Pakhtunkhwa, Pakistan.
2 Department of Zoology, Kohat University of Science and Technology, Kohat 26000, Khyber Pakhtunkhwa, Pakistan.
3 Institute of Microbiology, Gomal University, Dera Ismail Khan 29050, Khyber Pakhtunkhwa, Pakistan.
4 Faculty of Veterinary & Animal Sciences, Gomal University, Dera Ismail Khan 29050, Khyber Pakhtunkhwa, Pakistan.
Research Article
Comprehensive Research and Reviews in Life Sciences, 2022, 01(01), 007-013.
Article DOI: 10.57219/crrls.2022.1.1.0032
Publication history:
Received on 05 August 2022; revised on 09 September 2022; accepted on 11 September 2022
Abstract:
Wheat is most important component of food throughout the world. Wheat is full of different proteins but most abundant and most studied proteins are gliadin and glutenin. Interaction of gliadin and glutenin is important in biological properties of the wheat flour. Wheat also produce a toxin known as purothionin, which is used by the plant to show defense against different types of pathogen attack. Current in silico study was done to investigate the interaction between gliadin and glutenin proteins against wheat toxin alpha-purothionin solely. Methodology that was used in the current study consists of RaptorX tool for protein modeling, PROCHECK for predicted 3D model verification. CASTp 3.0 online tool for active site prediction. Online tool Cluspro and offline tool ligplus+v2.1 for protein-protein docking and visualization of docked complex respectively. Results showed high interaction between gliadin and glutenin, which supported the results of previous studies. While interaction between gliadin and purothionin proteins was high as compared to interaction between glutenin and alpha-purothionin proteins. Different helices were noted in the 3D structure of gliadin and glutenin proteins, where most of the time Gln amino acid was involved in making the helices. Form the results it has been concluded that greater interaction between gliadin and alpha-purothionin was due to similar sequence of gliadin with viral protein so the interaction of toxin purothionin against pathogens enhance the interaction of gliadin with alpha-purothionin. Current in silico study will enhance the understanding about the interaction of important wheat proteins.
Keywords:
Wheat; Gliadin; Glutenin; Alpha-purothionin
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