In silico modeling of lipase H

Abstract

LAH 2 is a type of autosomal recessive hypotrichosis that affect hairs, eyebrows, scalp and eyelashes. Mutations in Lipase H gene result in LAH 2. Changes that result from mutation on physiochemical properties, post-translational modifications, functional sites, secondary structure and tertiary structure lipase H gene (LIPH) at molecular level were analyzed in the current study. Results indicate that the 3rd motif of LIPH deletes as a result of mutation. The number of alpha helices and beta sheets become varied in normal and abnormal protein. Tertiary structure of LIPH was predicted through homology modeling. Mutations were then inserted to reveal the difference between normal and abnormal structure. Ligands to target LIPH are also retrieved. ASP178, ASP207 and HIS248 constitute the active site of LIPH. Missense mutations in LIPH also brought drastic changes at molecular level that led to imbalanced function. All these changes can be studied through bioinformatics without going for expensive laborious and time consuming experimental techniques.

Keywords: LAH2, LIPH, tertiary structure, secondary structure, physiochemical properties, ligands, active site

African Journal of Biotechnology Vol. 12(16), pp. 2051-2057