Computational interpretation and comparative annotation of lipocalin-2 protein having the candidate for antibacterial agent

Abstract

Recent studies have demonstrated that lipocalin-2 (LCN2) binds specifically with enterobactin to resist the bacterial infection in mammalian cells. The present study focuses on three key aspects, <i>viz</i>., diversity of bovine LCN2 in content with other mammalian groups, its structural variation and docking of bovine LCN2 with the scaffold proteins. Twenty nine sequences of LCN2 were selected for comparative annotation study using computational server and bioinformatic tools. Significant variations were found in physico-chemical properties and diversity in antigen binding sites between organisms. The homology model of the LCN2 from human and bovine illustrated the conformation of the best homology model. An attempt was made to determine binding affinities of bovine LCN2 with 1ZOK and 1PN5 through molecular modeling and docking. The aim of the study was not only to do comparative analysis, but also to find out how far LCN2 in bovine could be used as model for LCN2 proteins from other mammals. This may provide framework to develop the promising novel class of biopharmaceutical agents.