TaHSC70 gene of Triticum sp. is an associate of the heat shock protein family and plays a significant role in stress-related and defense responses educed by contagion with stripe rust fungus through a Jasmonic acid dependent signal transduction pathway. Hence, understanding molecular structure and function of the protein coded by this gene is of paramount importance for plant biologists working on stripe rust. The present study was aimed at sequence and in silico structural analysis of Hsp70 protein coded by this gene, through comparative modeling approach. Validation of the overall folds and structure, errors over localized regions and stereo chemical parameters was carried out using PDBSum server. Structure was a monomer with seven sheets, 1 β-α-βunit, 12 hairpins, 13β-bulges, 29 strands, 21 helices, 16 helix-helix interacs, 44 β-turns and 1 ϒ-turn. Two major domains were detected belonging to Hsp70 family while neural network analysis revealed protein to be highly phosphorylated at serine and threonine residues.
Key words: TaHSC70, Hsp70, Stripe rust, homology modelling, wheat.