1. In-silico analysis on human FTO and mutant S319F with various ligands for poly malformation syndrome.
- Author
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Priyanka and Anbarasu, K.
- Subjects
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ADIPOSE tissues , *LIGANDS (Biochemistry) , *MUTANT proteins , *MISSENSE mutation , *PROTEIN structure - Abstract
This research examines the structural stability of the mutant FTO protein, which is associated to obesity and mass, by employing molecular docking and the Autodock Vina tool. The Ingredients and Procedures: I have downloaded the protein structure from RCSB and UniProt PDB for the fat mass and obesity linked protein (FTO). We compiled a list of missense mutations that were found to have negative effects on fat mass and the obesity-associated protein (FTO) from the several SNP database systems. Following this, the SPDBV service was used to mutagenize the missense mutations. We performed molecular docking using PyRx, which operates on the autodock vina approach, after collecting the ligand's 3D structure from PubChem. Results: R316Q, S319F, and R322Q showed alterations and destructive effects on fat mass and obesity-associated protein structure, according to the expectations given by all the methodologies investigated for a disease. Conclusion: Using the PyRx online tools, we were able to find the best ligand that complements the protein's active areas and minimises the negative effects of FTO mutations on stability. Future molecular simulation and in vivo research aiming to create a therapy for poly malformation syndrome can take advantage of this. [ABSTRACT FROM AUTHOR]
- Published
- 2024
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