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EPX gene is a member of the peroxidase gene family and is expressed in eosinophils. The gene is found in a cluster of three peroxidase genes at chromosome 17q23.Mutations in this gene result in eosinophil peroxidase deficiency. Till date, there is very less work undertaken on the gene. Thus the current work aims to analyze and annotate the gene both sequentially and functionally. The work also includes the mutation analysis based on the variable sites present in the sequences when compared among the related organisms. The complete variation analysis along with the identification of possible deleterious mutations has been performed. As the structure of the protein is not reported in the literature, modeling approach was employed using modeler 9v3 to design its structure. The structure thus generated was also screened and validated for the quality using several parameters. The work can provide a stable platform for further investigation and research on EPX gene and its importance.
This gene is a member of the peroxidase gene family and is expressed in eosinophils. The encoded precursor protein is processed into covalently attached heavy and light chains to form the mature enzyme, which functions as an oxidant. The enzyme is released at sites of parasitic infection or allergen stimulation to mediate lysis of protozoa or parasitic worms. The gene is found in a cluster of three peroxidase genes at chromosome 17q23.Mutations in this gene result in eosinophil peroxidase deficiency.
The work involved the complete characterization of epx. Initially the sequence of the gene was retrieved from Gene cards database and the domains were identified using the SMART tool. The complete variability analysis was performed based on the results of MSA using CLUSTAW. The variability patterns were identified using a combination of the results obtained from RONN and SIFT. The work would provide an insight to the effect of change in the sequence on the tolerability, stability and functionality of the gene. The structure of the protein was modeled using Modeller 9v12 and the validation of the structural quality was performed in Saves server. The results of validation showed the quality of the structure to be 91.3% which indicates a very good structure for the sequence.
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