About CCMB

Scientist Details

Contact Details

Name : Rajan Sankaranarayanan

Room : E006

Telephone :
040-27192832 to 2835

Fax :
040-27160252,2716 0591

E-mail :

Research Interests

Structure of biomolecules dictates their function. The lab’s research interests are in trying to understand intermolecular recognition mechanisms. One major area of focus is on elucidating how very similar substrates are recognized with a high accuracy in order to achieve a faithful translation of the genetic code. Attempts are being made to elucidate the proofreading mechanisms during translation at atomic resolution and to provide a structural and functional proof for proofreading/editing defects leading to disease conditions like neurodegeneration. The other areas of research includes understanding the structural basis of complex lipid synthesis in Mycobacterium tuberculosis, structural basis of function of virulence factors from a rice pathogenic bacteria and calcium-binding proteins belonging to bg -crystallin family. Research work in the laboratory uses various tools, chiefly X-ray crystallography, to derive structural information and combines them with biochemical and functional data to understand the structural basis of function of various biomolecules.

Selected Publications

  • Ahmad, et al. (2013) Mechanism of chiral proofreading during translation of the genetic code. eLife 2, e01519.

  • Chhabra, A. et al. (2012) Nonprocessive [2+2]e- off-loading reductase domains from mycobacterial nonribosomal peptide synthetases. Proc. Natl. Acad. Sci. (USA) 109, 5681-5686.

  • Hussain, T. et al. (2010) Mechanistic insights into cognate substrate discrimination during proofreading in translation. Proc. Natl. Acad. Sci. (USA)107, 22117-22121.

  • Hussain, T. et al. (2006) Posttransfer editing mechanism of a D-aminoacyl-tRNA deacylase-like domain in threonyl-tRNA synthetase from archaea. EMBO J. 25, 4152-4162.

  • Dwivedi, S. et al. (2005) A D-amino acid editing module coupled to the translational apparatus in archaea. Nature Struct. Mol. Biol. 12, 556-557.

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