Structure prediction and docking-based molecular insights of human YB-1 and nucleic acid interaction |
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Authors: | Birendra Singh Yadav Swati Singh Amit Kumar Shaw |
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Institution: | 1. Department of Biotechnology, Motilal Nehru National Institute of Technology, Allahabad 211004, India;2. Center of Bioinformatics, Nehru Science Center, Institute of Interdisciplinary Studies, University of Allahabad, Allahabad 211002, India;3. Department of Biotechnology, National Institute of Technology, Durgapur 713209, India |
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Abstract: | Y-box-binding protein 1 (YB-1), a cold shock domain protein, is one of the most conserved nucleic acid-binding proteins. The multifunctional human YB-1 is a member of a large family of proteins with an evolutionary ancient cold shock domain. The presence of a cold shock domain is a specific feature of Y-box-binding proteins and allows attributing them to a wider group of proteins containing a cold shock domain. This protein is involved in a number of cellular processes including proliferation, differentiation and stress response. The YB-1 performs its function both in the cytoplasm and in the cell nucleus. In this study, we present the structure of full-length human YB-1 protein along with investigation of their nucleic acid-binding preferential. The study also focuses on biases for particular purine and pyrimidine bases. The overall goal of this study was to model and validate full-length YB-1 protein and to compare its nucleic acid-binding studies with previous reports. |
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Keywords: | YB-1 protein structure prediction cold shock domain docking |
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