Coordinated protein-protein interactions (PPIs) play an important role in majority of the biological processes. Studying protein-protein interactions is thus imperative to get a broader view of a biological process. PPIs have also been of special interest in the recent past as they represent important and novel drug targets for future therapeutic applications. A major focus of the research in my lab is to investigate role of PPIs that modulate transcription, electron transport and intercellular communications in bacteria. More ambitious goal is to identify and validate ‘hotspots’ on protein-protein interfaces that could be targeted for drug design. We use X-ray crystallography along with combination of other biophysical/biochemical techniques to reveal high resolution molecular details of proteins and protein-protein complexes and characterize their interactions.

• Priyanka, A., Solanki, V., Parkesh, R., and Thakur, K. G. (2016) Crystal structure of the N-terminal domain of human SIRT7 reveals a three-helical domain architecture. Proteins 84, 1558-1563.
• Mahor, D., Priyanka, A., Prasad, G. S., and Thakur, K. G. (2016) Functional and Structural Characterization of Purine Nucleoside Phosphorylase from Kluyveromyces lactis and Its Potential Applications in Reducing Purine Content in Food. PloS one 11, e0164279.
• Kaundal, S., Uttam, M., and Thakur, K. G. (2016) Dual Role of a Biosynthetic Enzyme, CysK, in Contact Dependent Growth Inhibition in Bacteria. PloS one 11, e0159844.
• Singh, P. K., Solanki, V., Sharma, S., Thakur, K. G., Krishnan, B., and Korpole, S. (2015) The intramolecular disulfide-stapled structure of laterosporulin, a class IId bacteriocin, conceals a human defensin-like structural module. The FEBS journal 282, 203-214.
• Kaur, G., Dutta, D., and Thakur, K. G. (2014) Crystal structure of Mycobacterium tuberculosis CarD, an essential RNA polymerase binding protein, reveals a quasidomain-swapped dimeric structural architecture. Proteins 82, 879-884.