School of Biotechnology

	Dr.R.SANKARANARAYANAN Reader M.Sc Computational Biology mail : rsankar1972@gmail.com	Publications   Previous Experience
Research Interests Tuberculosis (TB) is a highly contagious and a chronic respiratory disease caused by the human pathogen Mycobacterium tuberculosis (Mtb).   Although there are cock-tails of drugs currently available to cure this disease, the poor compliance of use of these drugs has given rise to a multi-drug resistant TB (MDR-TB) and an extensively drug resistant TB (XDR-TB). These forms of TB are virtually incurable.  According to the World Health Organisation (WHO) there were about 9.1 million new cases of TB and 1.4 million people died from this disease in 2007 alone. Among them 110,000 deaths were due to MDR-TB. TB is also a leading killer among HIV infected people.  These alarming statistics necessitate the urgent need for the development of new antibiotic drugs to cure this disease.   We are interested in structure elucidation of some functionally important proteins from Mtb.  My lab uses X-ray crystallographic technique to accomplish this task.  We are focusing on identifying and developing competitive inhibitors for Mtb proteins based on their crystal structures.  We also carry out molecular modeling/docking studies to augment the research in this bacterium.

Selected Publications Sankaranarayanan, R.,  Cherney, M.M.,  Garen, C.R., Garen, G., Niu, C., Yuan M. &  James, M.N. (2010).  The Molecular Structure of Ornithine acetyltransferase from Mycobacterium tuberculosis bound to Ornithine, a Competitive Inhibitor. J. Mol. Biol, 397, 979-990. Sankaranarayanan, R.,   Cherney, M.M., Cherney, L.T., Garen, C.R.,  Moradian, F. &         James, M. (2008). The Crystal Structures of Ornithine Carbamoyltransferase from Mycobacterium tuberculosis and Its Ternary Complex with Carbamoyl Phosphate and L-Norvaline Reveal the Enzyme’s Catalytic Mechanism.   J. Mol. Biol.  375, 1052-1063. Sankaranarayanan, R.,  Biswal, B.K. & Vijayan, M. (2005).  A new relaxed state in  horse methemoglobin characterized by crystallographic studies. Proteins, 60, 547-551. Sankaranarayanan, R., Garen,C.R., Cherney, M.M., Yuan, M., Lee, C. & James, M.N. (2009). Preliminary X-ray crystallgraphic analysis of ornithine     acetyltransferase (Rv1653) from Mycobacterium tuberculosis.  Acta Cryst. F65, 173-176. Witholt, S.J., Sankaranarayanan, R., Garen, C.R., Cherney, M.M., Cherney,  L.T.&  James, M.N.  (2008). Expression, purification, crystallization and preliminary X-ray     analysis of  Rv3117,  a probable thiosulfate sulfurtransferase (CysA3) from     Mycobacterium tuberculosis. Acta Cryst.  F64, 541-544. Kaushal, P.S., Sankaranarayanan, R. & Vijayan, M. (2008). Water-mediated variability in the structure of relaxed-state haemoglobin. Acta Cryst. F64, 463-469. Vijayakakshmi, L., Krishna, R., Sankaranarayanan, R. & Vijayan, M. (2008).  An Asymmetric Dimer of β-lactoglobulin in a Low Humidity Crystal Form.  Structural Changes that Accompany Partial Dehydration and Protein Action.  Proteins: Structure, Function and Bioinformatics,71,241-249 Murillo, A.C.,  Alber, T.C.,  Baker, E.N., Berger, J.M., Cherney, L.T., Cherney, M.M., Eisenberg, D., Garen, C.R., Hung, L.W., Ioerger, T.R., Jacobs, W.R., James M.N.G., Kim, C., Kriger, I., Li, H., Lott, J.S., Sankaranarayanan, R., Segelke, B.W., Terwilliger,       T.C., Wang,  F. & Sacchettini, J.C. (2007). High Throughput Crystallography of TB Drug Targets.  Infectious Disorder –  Drug Targets, 7, 127-139. Saraswathi, N.T., Sankaranarayanan, R. & Vijayan, M. (2002).  Effect of stabilizing additives on the structure and hydration of proteins: a study involving monoclinic lysozyme. Acta  Cryst. D58, 1162-1167.         Previous Experience Post Doctoral Research Experience: 2005 - 2010:    Prof. Michael James, FRS, Department of Biochemistry, University of    Alberta, Edmonton, Canada. 2001 -  2005:       Prof. M. Vijayan, Molecular Biophysics Unit, Indian Institute of Science, Bangalore.   Top

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