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Objective: To predict the tertiary structure of human interferon alpha/beta receptor 2 protein. Study Design: Structure prediction by using bio informatics tools. Place and Duration of Study: Department of Biochemistry, Swat Medical College (STMC), Saidu Shareef, Swat, Pakistan, from Aug 2019 to Dec 2019. Methodology: All protein sequences of human interferon alpha/beta receptor 2 (isoforma, b and c) (IFNAR-2) were retrieved through the BLAST search (The Basic Local Alignment Search Tool) from available databases ‘NCBI’ (National Centre for Biotechnology Information) and ‘Uni Prot KB’ (The Universal Protein Resource). Sequence alignment was conducted by using Clustal Omega, to get the consensus sequence for IFNAR-2 protein. Consensus protein sequence of human IFNAR-2 was used for the prediction of the three-dimensional structure by employing Swiss-Model Server. Moreover, subcellular localization analysis was also performed by using CELLO2GO program. Results: Structural model of human IFNAR-2 protein was predicted and evaluated by Ramachandran dimension. Cellular localization of tertiary topological domains of the predicted models were revealed probability of localization of IFNAR-2 protein (isoform a, b & c) is highest in the plasma membrane due to the presence of the transmembrane alpha helical regions. Conclusion: This study predicted the tertiary structural dimensions of human IFNAR-2 protein, including the specific topological domains that contribute towards the subcellular compartmentalization and functional characteristics.

Objective: To study the functional and molecular interactions of IFNAR-2 within biological networks Study Design: Computational analysis: STRING software Place and Duration of Study: Department of Biochemistry, HITEC-Institute of Medical Sciences, Taxila Cantt, Pakistan, from Dec 2017 to Jun 2018. Methodology: Protein sequence of IFNAR-2 protein was obtained from ‘National Centre for Biotechnology Information (NCBI)’ database and STRING analysis conducted by applying specific parameters including (1) Text mining (2) Experiments (3) Databases (4) Co-expression (5) Neighborhood (6) Gene fusion and (7) Co-occurrence for identifying protein-protein interactions and molecular associations. Maximum number of interactors was set at 20 and highest confidence level was set at 0.900. Results: Protein-protein interaction analysis translate that human IFNAR-2 protein has high level of interactions with a set of proteins of similar size, drawn from the genome. This set represents a partial biologically connected group of proteins. This information has a potential to set the basis for further experimental investigations in more integrated and biologically linked pathway-oriented perspective that results in more targeted outcomes. Conclusion: Functional and molecular enrichment through STRING analysis revealed that IFNAR-2 protein has strong associations and serves as a key player in antiviral response of immune system.