In silico characterization and structural modeling of a homeobox protein MSX1 from Homo sapiens

Abstract

Abstract Introduction MSX1 protein, a homeobox transcriptional regulator plays a significant role in various developmental processes of the mammalian system such as limb-pattern formation, craniofacial development, in particular, odontogenesis, and tumor growth inhibition. Several studies have been performed on MSX1 at the genomic and transcriptomic levels. However, there is a lack of information on its structural and conformational aspects. Objective For better understanding of the molecular mechanism of MSX1, the present study aims to conduct a detailed in-silico analysis of this protein in terms of its physicochemical properties, secondary and tertiary structure predictions, interacting partners, and phylogenetic relationship with other orthologs. Methods The sequence of the MSX1 protein from Homo sapiens was retrieved in the FASTA format from the National Center for Biotechnology Information (NCBI). The standard bioinformatic tools were further used to characterize and model the structure of this protein. Results The in-silico characterization of MSX1 revealed that it is a basic, non-polar, and thermostable globular protein mainly localized in the nucleus. This protein is extremely rigid due to the presence of high proline content. The phylogenetic and synteny analysis revealed that the gene is highly conserved at the level of the amino acid sequences, but underwent several modifications at the genomic level in the course of evolution possibly to attain the diverse function. Major part of this protein is a random coil, making it suitable for interaction with other proteins. Subcellular localization and protein-protein interaction suggested that the protein may act as a secretory protein and play a crucial role in regulating several developmental processes. Docking analysis suggested that the MSX1 protein may interact with other proteins and form complexes to carry out its function. Conclusion The structural characterization of this protein will help to better understand its molecular mechanism of action. In addition, the predicted 3-D model would act as a base for further understanding of the protein s other functional potential.