Introduction: In nature, plants are frequently exposed to drought and bacterial pathogens simultaneously. Calmodulin-binding Protein 60 g (CBP60g) is transcription factor. under combined stress, drought through the ABA pathway downregulates the induction of Calmodulin-binding Protein 60 g (CBP60g) and Systemic Acquired Resistance Deficient 1 (SARD1), two transcription factors crucial for SA production upon bacterial infection. Due to the important role of CBP60g, it is important to investigate the secondary and tertiary structure of this receptor. Predicting of the secondary and tertiary structure of proteins is very important in subsequent protein studies and the study and identification of the function of unknown proteins. Predicting the tertiary structure of proteins can also be used in molecular docking.
Methods: In this study, the Phyre2 software was used to investigate the secondary structure of the CBP60g protein. Three-dimensional structure modeling was performed based on the selection of a pattern with a high resemblance to the target protein using the Swiss Model database.
Results: The results indicate that 6 similar structures were found in the protein database for CBP60g, one of these structures, called the crystal structure of a c6tmiB, had a similarity of 25%. The model chosen for modeling CBP60g protein in Protein Calmodulin-binding protein 60 G AlphaFold DB model of CB60G_ARATH (gene: CBP60G, organism: Arabidopsis thaliana (Mouse-ear cress)) (F4K2R6.1.A) contains 563 amino acids and discovered by AlphaFold v2 with a resolution 3.30 angstroms. The Identity F4K2R6.1.A of pattern with target, protein is 100.
Conclusion: The results of this research can be used in future research and molecular docking and provide basic information to investigate other immune receptors.
Keywords: Receptor, FLS2, 3D structure, 2D structure, Swiss Model Phyre2, Docking