Amino Acids

, Volume 50, Issue 5, pp 593–607 | Cite as

Characterization of structural and functional role of selenocysteine in selenoprotein H and its impact on DNA binding

  • Sagar H. BarageEmail author
  • Deepti D. Deobagkar
  • Vijay B. BaladhyeEmail author
Original Article


Selenoproteins are a group of proteins which contain selenocysteine (Sec or U) in their primary structure. Selenoproteins play a critical role in antioxidant defense, hormone metabolism, immune responses and muscle development. The selenoprotein H (SELENOH) is essential in the regulation of gene expression in response to redox status and antioxidant defense. It has Sec residue located in conserved CXXU motif similar to other selenoproteins. However, exact biological function of Sec residue in SELENOH is not known in detail. Therefore, it is essential to understand the structural and functional role of Sec in SELENOH. In the present study, homology modelling and MD simulation were performed to understand the role of Sec residue in SELENOH. The modelled 3D structure of wild-SELENOH along with two mutants (Mut-U44C and Mut-41CS–SC44) was subjected to MD simulation. Based on simulation results, we demonstrate that wild-SELENOH structure is dynamically stabilized by network of intramolecular hydrogen bonding and internal residue contacts facilitated by Sec residue. In contrast, notable differences have been observed in residue contacts and stability in other two mutant structures. Additionally, docking studies revealed that 3PRGRKRK9 motif of wild-SELENOH interacts with HSE and STRE of DNA molecule as observed experimentally. Similar to earlier reports, our sequence analysis study pinpoints conserved 3PRGRKRK9 motif present in SELENOH perform dual role as AT-hook motif and NLS. Overall, the obtained results clearly illustrate Sec residue plays an important role to restore functionally active conformation of SELENOH. The present study broadened our current understanding regarding the role of selenocysteine in protein structure and function.


Selenocysteine Selenoprotein H MD simulation Molecular docking DNA binding 



SHB gratefully acknowledges DST-SERB for providing research grant under young scientist scheme (YSS/2015/0001030). The authors are thankful to Bioinformatics Centre, Savitribai Phule Pune University, Pune for infrastructure support.

Compliance with ethical standards

Conflict of interest

The authors declare that they do not have any conflict of interest.

Research involving human participants and/or animals

This article does not contain any studies with human participants or animals performed by any of the authors.

Informed consent

Informed consent was obtained from all individual participants included in the study.

Supplementary material

726_2018_2543_MOESM1_ESM.docx (3.7 mb)
Supplementary material 1 (DOCX 3837 kb)


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Copyright information

© Springer-Verlag GmbH Austria, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Bioinformatics CentreSavitribai Phule Pune UniversityPuneIndia
  2. 2.ISRO Chair ProfessorSavitribai Phule Pune UniversityPuneIndia

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