G Senthil Kumar

Staff Scientist IV, BRIC-NII

Profile

The major focus of the laboratory is to characterize the molecular basis for the interactions between pathogens (that include bacteria and viruses) and antibodies (that are the critical components of the immune system that helps to neutralize the effect of pathogens). Antibodies recognize a unique molecule of the pathogens, called antigen (Ag), with high affinity and specificity. Hence, the characterization of the region in the pathogens (called epitopes) that interacts with the antibodies is crucial for vaccine design. Furthermore, the importance of protein dynamics, besides the structure, in the function of intermolecular interactions is well-recognized. To this end, our laboratory is interested in the characterization of the role of structural and dynamic changes induced as a result of antigen-antibody interactions using a combination of biochemical, biophysical, and immunological techniques.

Current Focus Areas

  • Structure-based design of small molecule inhibitors that target the E protein of DENV

  • Development of Synthetic Binding Proteins as Antibody Mimetic

  • Structural and Dynamic studies of SARS-CoV-2 proteins

  • Role of Dynamics in antigen-antibody interactions

Selected Publications

  • Kumar GS, Clarkson MW, Kunze MBA, Granata D, Wand AJ, Lindorff- Larsen K, Page R and Peti W. (2018) Dynamic activation and regulation of the mitogen-activated protein kinase p38, Proc. Natl. Acad. Sci. USA., 115 (18), 46550-4600.

  • Kumar GS, Gokhan E, Munter S, Bollen M, Vagnarelli P, Peti W and Page R. (2016) The Ki-67 and RepoMan mitotic phosphatases assemble via an identical, yet novel mechanism, eLife, 5: e16539.

  • Kumar GS*, Page R and Peti W.* (2021) The interaction of p38 with its upstream kinase MKK6, Protein Sci. 30(4), 908-913. (*Co-corresponding Authors)

  • Kumar GS, Choy MS, Koveal D, Lorinsky MK, Lyons SP, Kettenbach AN, Page R and Peti W. (2018) Identification of the substrate recruitment mechanism of the muscle glycogen protein phosphatase-1 holoenzyme, Science Advances, 4, eaau6044.

  • Kumar GS, Page R and Peti W. (2020) The mode of action of the Protein tyrosine phosphatase 1B inhibitor Ertiprotafib, PLOS One. 15(10), e0240044.

Skills & Proficiency

Protein-protein interactions NMR Spectroscopy X-ray Crystallography Antigen-antibody interactions Epitope/paratope mapping Structure-function relationship studies Structural dynamics Host-pathogen interactions Molecular Dynamics Simulations DENV RSV
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