The effects of a stomach flu can range from pesky to deadly. Researchers recently used an AI program to predict the structure of a common rotavirus and collaborated with a Biosciences researcher working at the Advanced Light Source to validate their novel finding.
Researchers from the Baylor College of Medicine employed previously constructed DNA-encoded chemistry technology (DEC-tec) libraries to identify several candidate molecules that could inhibit the action of Mpro, the main protease of SARS-CoV-2. In a recent study, the researchers described CDD-1713, a new inhibitor to the enzyme Mpro that is involved in propagating the virus. The X-ray crystallographic data, which was collected by Banumathi Sankaran in the Molecular Biophysics and Integrated Bioimaging Division, allowed the researchers to determine that CDD-1713 inhibits the activity of Mpro by binding in the active site of this enzyme.
A team of scientists led by David Baker at the University of Washington developed a method to design artificial proteins to serve as a framework for viral antigens. Their study was published recently in the journal eLife. Berkeley Lab scientists collected data at the Advanced Light Source to visualize the atomic structure and determine the dynamics of the designed scaffolds.
Combining cryo-electron microscopy, biochemical assays, and protein crystallography at Advanced Light Source (ALS) Beamline 5.0.2 (part of the Berkeley Center for Structural Biology), researchers from the Baylor College of Medicine discovered that rotavirus VP3 incorporates in one place all the enzymatic activities required to effectively cap rotavirus mRNA, making it unique among viral-capping enzymes.
The crystallographic study of STING (stimulator of interferon genes), a transmembrane protein that plays a key role in innate immunity, in complex with TBK1 (serine/threonine-protein kinase), an enzyme that regulates the inflammatory response to foreign DNA, is extremely challenging due to weakly diffracting crystals. But thanks to the expertise of Berkeley Center for Structural Biology (BCSB) scientists, researchers from Texas A&M University (TAMU) were able to pinpoint the conserved motif of STING that mediates the recruitment and activation of TBK1. They published their results in Nature.