SEQUENCE ANALYSIS AND STRUCTURAL CHARACTERIZATION OF TISSUE TRANSGLUTAMINASE 2(TG2) BY IN SILICO APPROACH
DOI:
https://doi.org/10.22159/ijpps.2017v9i10.20353Keywords:
Tissue transglutaminase 2, Metastasis, Sequence alignment, Phylogenetic analysis, BLAST, Stereochemical parameter, Phosphorylation, HydropathicityAbstract
Objective: TG2 is multifunctional protein. The up regulation leads into different pathological disorders. The objective of the present study was the prediction of a structural feature of TG2 (Tissue transglutaminase) protein with in silico approach.
Methods: In this study, we have investigated the structural feature of TG2 by using various biological databases (uniprot, NCBI, Pfam) and online tools such as BLAST, PDBsum, protoparam tools.
Results: The predicted structure of TG2 protein has shown that amino acid residues conserved throughout the sequence in selected mammals. During the course of evolution, mammalian TG2 protein is orthologus; human TG2 shares its characters with chimpanzee while mice and rat were closely related to each other. This protein was mainly cytosolic but also present in other cell organalles. It has four catalytic domains and three active sites with multiple metal binding domain specifically for calcium. The pI value was 5.11, GRAVY-0.283. The phosphorylation sites were present at serine and threonine. The structure was a monomer with 14 alpha helices and 9 sheets. Ramachandran plot showed about 98% residues in the favoured region.
Conclusion: Collectively, these data suggest that the predicted TG2 protein may act as a good therapeutic target. Targeting phosphorylation sites may help in down regulation of TG2. The modelled protein can be used for further work.
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