In silico prediction of structure and functions for some proteins of male-specific region of the human Y chromosome

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• 作者：Chinmoy Saha (1) (2)
  Ahsan Habib Polash (1)
  Md. Tariqul Islam (1)
  Farhana Shafrin (1)
  
• 关键词：male specific region ; Y chromosome ; homology modeling ; structural domain ; protein functions
• 刊名：Interdisciplinary Sciences: Computational Life Sciences
• 出版年：2013
• 出版时间：December 2013
• 年：2013
• 卷：5
• 期：4
• 页码：258-269
• 全文大小：875 KB
• 作者单位：Chinmoy Saha (1) (2)
  Ahsan Habib Polash (1)
  Md. Tariqul Islam (1)
  Farhana Shafrin (1)
  
  1. Molecular Biology Lab, Department of Biochemistry and Molecular Biology, University of Dhaka, Dhaka, 1000, Bangladesh
  2. Department of Genetic Engineering and Biotechnology, Shahjalal University of Science and Technology, Sylhet, 3114, Bangladesh
  
• ISSN：1867-1462

文摘

Male-specific region of the human Y chromosome (MSY) comprises 95% of its length that is functionally active. This portion inherits in block from father to male offspring. Most of the genes in the MSY region are involved in male-specific function, such as sex determination and spermatogenesis; also contains genes probably involved in other cellular functions. However, a detailed characterization of numerous MSY-encoded proteins still remains to be done. In this study, 12 uncharacterized proteins of MSY were analyzed through bioinformatics tools for structural and functional characterization. Within these 12 proteins, a total of 55 domains were found, with DnaJ domain signature corresponding to be the highest (11%) followed by both FAD-dependent pyridine nucleotide reductase signature and fumarate lyase superfamily signature (9%). The 3D structures of our selected proteins were built up using homology modeling and the protein threading approaches. These predicted structures confirmed in detail the stereochemistry; indicating reasonably good quality model. Furthermore the predicted functions and the proteins with whom they interact established their biological role and their mechanism of action at molecular level. The results of these structure-functional annotations provide a comprehensive view of the proteins encoded by MSY, which sheds light on their biological functions and molecular mechanisms. The data presented in this study may assist in future prognosis of several human diseases such as Turner syndrome, gonadal sex reversal, spermatogenic failure, and gonadoblastoma.