Comparison of Wild Type and Mutated (mHuIFN-β 27-101) Interferon Binding to the IFNRA Receptor by Molecular Docking
Introduction: Interferon beta is one of the members of type I interferons. Creating R27T and V101F mutations is one of the important researches performed to improve function, decrease immunogenicity, increase expression and increase half-life of interferon beta. In this study, the effects of R27T an...
| Main Authors: | , |
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| Format: | Article |
| Language: | fas |
| Published: |
Kerman University of Medical Sciences
2018-12-01
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| Series: | مجله انفورماتیک سلامت و زیست پزشکی |
| Subjects: | |
| Online Access: | http://jhbmi.ir/article-1-328-en.html |
| Summary: | Introduction: Interferon beta is one of the members of type I interferons. Creating R27T and V101F mutations is one of the important researches performed to improve function, decrease immunogenicity, increase expression and increase half-life of interferon beta. In this study, the effects of R27T and V101F mutations on interferon beta binding to interferon receptors were studied by molecular docking.
Method: This study was performed through Bioinformatics methods. The required crystal structures were provided by the RCSB server. The simulations of R27T and V101F mutations were performed using online Rosetta Backrub software. Comparison of access to the solvent for the amino acids in the created structures was performed using asaview online server. Also, the effect of mutations on the structure and protein folding was investigated by the online Hope server and SPDBV software. The molecular docking between HuIFN-β and the external region of IFNAR receptor was performed using the online ClusPro2 protein-protein docking server.
Results: The comparison of the values of the negative binding energy (ΔGbind) obtained from protein-protein molecular docking between IFNAR receptor and HuIFN-β, mHuIFN-β-27, mHuIFN-β-101 and mHuIFN-β-27-101 ligands did not show a significant difference (P> 0.99).
Conclusion: Regarding these results, it can be concluded that the produced mutations do not have a negative effect on the forming of rHuIFN-β/IFNAR complex and does not interfere with the binding of the interferon beta to the receptor and thus improves the quality of the produced rHuIFN-β. |
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| ISSN: | 2423-3870 2423-3498 |