Genentech researchers used a suite of methods, including small-angle X-ray scattering (SAXS) at the Advanced Light Source (ALS) to learn how an assembly of three proteins works together to transmit signals for cell division. The work reveals new targets for the development of drugs that fight certain types of cancer, including lung, colorectal, and pancreatic.
Deconstructing the Infectious Machinery of the SARS-CoV-2 Virus
Scientists from three national laboratories who specialize in revealing the atomic structure of proteins collaborated to model the complex protein responsible for SARS-CoV-2 replication, revealing potential weak spots for drug development.
Shape-shifting Protein Helps SARS-CoV-2 Evade Human Immune Defenses
Papain-like protease (PLpro) from SARS-CoV-2 plays essential roles in the replication cycle of the virus that is the cause of the global COVID-19 pandemic. In human cells that the virus has infected, PLpro seeks out and binds with the interferon-stimulated gene 15 (ISG15) protein, a key component of the cells’ immune response. PLpro strips ISG15 from other cellular proteins to aid SARS-CoV-2 in evading the body’s immune system.
Scientists at Oak Ridge National Laboratory (ORNL) used small-angle neutron scattering (SANS) at the High Flux Isotope Reactor (HFIR) combined with computational techniques to reveal the molecular details of how the two proteins interact. Susan Tsutakawa, a staff scientist in the Molecular Biophysics and Integrated Bioimaging (MBIB) Division, obtained small-angle x-ray scattering (SAXS) data on the PLpro-ISG15 complex at Berkeley Lab’s Advanced Light Source (ALS) to augment the SANS work.
Study Finds ‘Missing Link’ in the Evolutionary History of Carbon-Fixing Protein Rubisco
In a study appearing in Nature Plants, researchers from UC Davis, UC Berkeley, and Berkeley Lab report the discovery and characterization of a previously undescribed lineage of form I rubisco – one that the researchers suspect diverged from form I rubisco prior to the evolution of cyanobacteria. The novel lineage, called form I’ rubisco, gives researchers new insights into the structural evolution of form I rubisco, potentially providing clues as to how this enzyme changed the planet.
The work was led by Patrick Shih, a UC Davis assistant professor and the director of Plant Biosystems Design at the Joint BioEnergy Institute (JBEI), and Doug Banda, a postdoctoral scholar in his lab.
Enigmatic Protein Sculpts DNA to Repair Damage
Biosciences Area researchers and their collaborators have determined how a protein called XPG binds to and reshapes damaged DNA, illuminating its role in averting genetic disease and cancer.
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