Molecular interactions control every aspect of cellular function. Therefore, decoding protein-protein, protein-nucleic acid, and protein-ligand interactions is critical for comprehending any cellular event. Knowing how these interactions are perturbed in various disease conditions is crucial for developing effective therapeutics and drugs. To gain such molecular insights, multiple high-resolution structures of various macromolecular complexes are required. Therefore, along with conventional molecular biology, biochemistry, and biophysical techniques, we employ cryo-electron microscopy (cryo-EM) and X-ray crystallography to determine atomic or near-atomic structures. With this, we aim to advance the structural knowledge crucial to comprehending the biophysical and biochemical aspects of protein structure and function. Current projects in the lab as as follows:
1: Elucidating the molecular design principles underlying variable substrate recruitment by PP2A holoenzymes.
2:Understanding the role of protein-protein interactions in the bacterial innate immune system using single-particle cryo-electron microscopy.
3:Structural biology of signal transmission and epigenetic gene regulation.