Functional insights by comparison of modeled structures of 18kDa small heat shock protein and its mutant in Mycobacterium leprae.

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-ter

SUBMITTER: Rehna EA 

PROVIDER: S-EPMC2646194 | biostudies-literature | 2008

REPOSITORIES: biostudies-literature