Abstract
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.
Highlights
Tissue transglutaminase 2 (TG2) is a calcium-dependent cellular matrix protein ubiquitously expressed member of the large family of transglutaminases [1]
After protein database search the amino acid sequence of TG2 protein was retrieved from Uniprot
For the present study mammalian organisms; Human, Chimpanzee, Bovine, European polecat, Pig, Mice, Chick were selected. The reason for this selection for analysis is, because target protein is predominant in the mammals and the study would help to understand the conserved domain and evolutionary relationship of human TG2 with the selected mammals
Summary
Tissue transglutaminase 2 (TG2) is a calcium-dependent cellular matrix protein ubiquitously expressed member of the large family of transglutaminases [1]. TG2 is the most extensively studied member and biologically characterized, because it performs multiple functions and present in the wide spectrum of living organisms such as microorganism, invertebrates, birds, mammals and predominantly in human beings [3]. In the humans, it is mainly found in both intracellular and extracellular locations, including cytosol, nucleus, endoplasmic reticulum, mitochondria, extracellular matrix, focal adhesion area, and as an intrinsic component of the plasma membrane [4]. TG2 interacts with both intra and extracellular proteins and alters their structure and functions
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