Journal of Agriculture

Yazarlar: Fatih DEMİREL

Konular:Mühendislik, Ziraat

DOI:10.46876/ja.846023

Anahtar Kelimeler:Soybean,Protein disulfide isomerase (PDI),In silico,Protein-protein docking

Özet: Protein disulfide isomerases are molecular chaperones containing the thioredoxin domain that are involved in the correct formation of disulfide bonds during the protein folding process. There are many studies investigating the catalytic and chaperone roles of PDI proteins in animals. Studies on the diversity and function of PDI proteins in plants are limited. In this study, the presence of 12 PDI genes in the soybean genome was shown with reference to the Arabidopsis PDI gene. The properties of the proteins belonging to these genes were revealed by in silico approaches. It was found that the active site-WCXXC motif was not conserved in the GmPDI6c and GmPDI6d proteins, but this sequence was present in other proteins. As a result of protein modeling, the protein with the highest GMQE score among soy PDI proteins was taken into consideration and its interaction with the coat protein of Tobacco ringspot virus was revealed through docking. The in silico analysis results obtained from the study need to be verified by experimental approaches.

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