Journal of Molecular Modeling

, Volume 17, Issue 2, pp 251–263

Insight into residues involved in the structure and function of the breast cancer associated protein human gamma synuclein

  • Panneerselvam Manivel
  • Jayaraman Muthukumaran
  • Muthu Kannan
  • Ramadas Krishna
Original Paper

DOI: 10.1007/s00894-010-0718-4

Cite this article as:
Manivel, P., Muthukumaran, J., Kannan, M. et al. J Mol Model (2011) 17: 251. doi:10.1007/s00894-010-0718-4

Abstract

Aberrantly expressed human gamma synuclein (SNCG) interacts with BubR1 and heat shock protein 70 (Hsp70) in late stages of breast and ovarian cancer. This interaction is essential for progression, development and survival of cancer cells. A short, synthetically designed ankyrin-repeat-containing peptide (ANK peptide) was proven to inhibit the activity of SNCG. However, the potential binding site residues of SNCG responsible for its oncogenic function have not been reported so far. The objectives of this study were to generate a three-dimensional model of SNCG and to identify the key residues involved in interaction with BubR1, ANK peptide and Hsp70. Our study is the first attempt to report the specific binding of SNCG with the TPR motif of BubR1 and the 18kDa region of Hsp70. Our findings provide novel insights into the mechanism of interaction of SNCG, and can act as a basis for the ongoing drug design and discovery process aimed at treating breast and ovarian cancer.

Keywords

Human gamma synuclein BubR1 Hsp70 ANK peptide Breast cancer 

Copyright information

© Springer-Verlag 2010

Authors and Affiliations

  • Panneerselvam Manivel
    • 1
  • Jayaraman Muthukumaran
    • 1
  • Muthu Kannan
    • 1
  • Ramadas Krishna
    • 1
  1. 1.Centre of Excellence in Bioinformatics, School of Life SciencesPondicherry UniversityPuducherryIndia

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