Research Article Open Access

Modeling and Molecular Docking Studies on Rnase Aspergillus niger and Leishmania donovani Actin: Antileishmanial Activity

Ravi Kumar Gundampati1, Shraddha Sahu1, Kirti Shila Sonkar1, Mira Debnath1, Avinash Kumar Srivastava1 and Medicherla Venkata Jagannadham1
  • 1 Banaras Hindu University, India

Abstract

A.niger Rnase was designed from ACTBIND (PDB ID: 3D3Z). Yeast actin-human gelsolin segment 1 complex (PDB ID: 1YAG) was used as template for L. donovani actin protein for 3D model in Modeller9v8. These models were testified by PROCHECK, ERRAT, WHAT-IF, PROSA2003 and VERIFY-3D. All evidences suggest that the geometric quality of the backbone conformation, energy profile, residue interaction and contact of the structures were well within the limits of reliable structures. The interaction energy of docking was calculated using the HEX server. Etotal and calculated RMSD values were -1.902, -9.323 kcal moL-1 and 0.402 Å, respectively. The study presented here has an advantage to design molecules that may have antileishmanial activity.

American Journal of Biochemistry and Biotechnology
Volume 9 No. 3, 2013, 318-328

DOI: https://doi.org/10.3844/ajbbsp.2013.318.328

Submitted On: 14 June 2013 Published On: 21 September 2013

How to Cite: Gundampati, R. K., Sahu, S., Sonkar, K. S., Debnath, M., Srivastava, A. K. & Jagannadham, M. V. (2013). Modeling and Molecular Docking Studies on Rnase Aspergillus niger and Leishmania donovani Actin: Antileishmanial Activity. American Journal of Biochemistry and Biotechnology, 9(3), 318-328. https://doi.org/10.3844/ajbbsp.2013.318.328

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Keywords

  • A. niger Rnase
  • Leishmania Donovani Actin
  • Protein-Protein Docking
  • Modeller9v8
  • Hex Server
  • Novel Target For Leishmanisis