Research
Structure and signal transduction of G-protein coupled receptors
G-protein coupled receptors (GPCRs) are marvels of structural biology, their intricate three-dimensional architecture allowing them to serve as molecular sentries on the cell's surface. Embedded in the cell membrane, each GPCR is a twisting, snake-like protein structure meticulously sculpted to bind specific signaling molecules. When these molecular messengers arrive, they induce conformational shifts that ripple through the GPCR's structure. This change in shape activates signaling pathways inside the cell, orchestrating cellular responses.
Unraveling the structural mysteries of GPCRs has been a major frontier in biology. Using techniques like X-ray crystallography and cryo-electron microscopy, we are planing to map the three-dimensional folds and motions of these molecular machines and provide insights into their binding pockets, activation mechanisms, and interactions with signaling partners.
Structures of viral proteins and receptors, and the mechanism of infection
Viruses are ancient hijackers, molecular pirates that have evolved intricate structural tricks to board and commandeer the cellular ships of living organisms. At the vanguard of this viral invasion force are the viral surface proteins - elaborately folded molecular machines that allow viruses to latch onto and infiltrate their host cells. Like precision surgical tools, these proteins are structurally sculpted to recognize and bind specific receptor molecules on the target cell's exterior.
Revealing the atomic structures of viral proteins and their cellular receptors has been a cardinal quest in structural virology. Through techniques like X-ray crystallography and cryo-electron microscopy, we are planning to elucidate the three-dimensional structures of these molecules. Intricate binding pockets, flexing molecular hinges, and conformational changes will be revealed. Such structural insights have proven indispensable for vaccine design and antiviral drug development, allowing researchers to disrupt the molecular interactions between virus and host. As we continue deconstructing the structural mechanisms of viral infection, we move closer to fortifying our cellular defenses against these pathogens.
Structures and mechanism of transporters
The membrane is studded with an array of molecular transporters. These transporters exhibit an astonishing structural diversity, their three-dimensional folds precisely sculpted to facilitate the translocation of specific substrates.
Biophysical techniques such as X-ray crystallography and cryo-electron microscopy can be used to illuminate the structural dynamics of these molecular machines, unveiling their substrate-binding pockets, conformational cycling, and cooperative motions. These structural insights will fuel structure-guided approaches to drug design and membrane protein engineering for biomedical and biotechnological applications