Abstract
In this work we are proposing Homology modeled structures of Mycobacterium leprae 18kDa heat shock protein and its mutant. The more closely related structure of the small heat shock protein (sHSP) belonging to the eukaryotic species from wheat sHSP16.9 and 16.3kDa ACR1 protein from Mycobacterium tuberculosis were used as template structures. Each model contains an N-terminal domain, alpha-crystalline domain and a C-terminal tail. The models showed that a single point mutation from serine to proline at 52(nd) position causes structural changes. The structural changes are observed in N-terminal region and alpha-crystalline domains. Serine in 52(nd) position is observed in beta4 strand and Proline in 52(nd) position is observed in loop. The number of residues contributing alpha helix at N-terminal region varies in both models. In 18S more number of residues is present in alpha helix when compared to 18P. The loop regions between beta3 and beta4 strands of both models vary in number of residues present in it. Number of residues contributing beta4 strand in both models vary. beta6 strand is absent in both models. Major functional peptide region of alpha crystalline domains of both models varies. These differences observed in secondary structures support their distinct functional roles. It also emphasizes that a point mutation can cause structural variation.