@article{Trali_Javed_Sadiq_2018, title={AN IN SILICO PRIMARY AND SECONDARY STRUCTURE PREDICTION OF HUMAN INTERFERON ALPHA RECEPTOR 2 PROTEIN}, volume={14}, url={https://pjp.pps.org.pk/index.php/PJP/article/view/278}, abstractNote={<p><strong>Background:</strong> Structural analysis of human interferon alpha receptor 2 (IFNAR-2) protein is important to determine its structure and function because that information is needed to understand the role and mechanism of IFNAR-2 protein in human immune system. Therefore, this study was conducted to find out composition of amino acids contributing in primary and secondary structure of IFNAR-2 protein. <strong>Methods:</strong> Protein sequences of human IFNAR-2 were retrieved from ‘The Universal Protein Resource (UniProt)’ and ‘National Center for Biotechnology Information (NCBI)’ databases. The Basic Local Alignment Search Tool (BLAST) was used to search for every IFNAR-2 protein sequence in NCBI database. Human IFNAR-2 protein sequences were further refined according to set criteria for experimental analysis. All retrieved IFNAR-2 protein sequences were aligned by using computational tool ‘Clustal Omega’. Consensus protein sequence was obtained from aligned protein dataset. Furthermore, consensus protein sequence of IFNAR-2 was subjected for secondary structure prediction analysis. Protein topology was predicted by using Expert Protein Analysis System (ExPASy) server and Transmembrane Helices; Hidden Markov Model. <strong>Results:</strong> Alignment data set revealed that IFNAR-2 protein consisted of 515 amino acids long chain, having total 37 identical positions with 6.446% identity. Protein topology analysis predicted that human IFNAR-2 protein consists of verities of secondary structures such as alpha-helix, turn and beta sheets. Alpha-helixes mainly form three topological domains (i) inner (1–6 amino acids), (ii) outer (7–29 amino acids) and (iii) trans-membrane domain (30–515 amino acids). <strong>Conclusion:</strong> Human IFNAR-2 protein consists of 515 amino acids having hydrophobic, polar and aromatic characteristics. Alpha-helixes, turn, beta sheets and three topological domains constitute secondary structure and predicted topological domains contribute in the subcellular compartmentalization.</p> <p><strong>Pak J Physiol 2018;</strong>14(1):40–3</p>}, number={1}, journal={Pakistan Journal of Physiology}, author={Trali, Gulshan Ara and Javed, Ambreen and Sadiq, Alia}, year={2018}, month={Mar.}, pages={40–3} }