The hepatitis C virus (HCV), which attacks the liver, is known to repurpose host-cell components known as microRNAs—short RNA strands that act to silence gene expression. Now, the molecular structure of an HCV site bound to a microRNA complex revealed how their interactions shield the virus from the host cell’s protective response. Read more »
ALS Work Using Protein Crystallography
Protein crystallography is used for determining the molecular structure of proteins. Crystallized protein molecules cause a beam of incident x-rays to scatter in many directions, with constructive and destructive interference generating a diffraction pattern. By analyzing these patterns, a crystallographer can produce a three-dimensional picture of the density of electrons within the crystal and thus determine the protein's structure.
Programmable stiffness and stress–relaxation of cross-linked self-assembling peptide hydrogels
An AFM image representing a supramolecular hydrogel based on a cross-linked self-assembling peptide (SAP). Cross-linking allows for precise tuning of biomechanical properties, spanning the range of stiffness values found in the human central nervous system, pancreas, liver, lung, and skin tissues. The findings provide a new strategy helpful for soft tissue regeneration. Read more »
DNA Synthesis: Flip It and Reverse It
What if the current model for DNA synthesis were flipped on its head? Using time-resolved x-ray crystallography, researchers gained new insights into this essential biological process, revealing that two steps in the synthesis pathway are, in reality, reversed. Read more »
An Antibody That Broadly Neutralizes SARS-CoV-2
An antibody that appears to neutralize all known SARS-CoV-2 strains and closely related coronaviruses was discovered with the help of the ALS. The work highlights principles underlying antibody potency, breadth, and escapability that can guide the development of therapeutics against the current and potential future pandemics. Read more »
Sounding the Antiviral Alarm: A New Family of Immune-System Sensors
Comparison of enzyme structures from humans and insects revealed a new family of evolutionarily related immune-system sensors, triggered by viral RNA or DNA to produce tailored signals that initiate antiviral action. The results shed new light on the diversity and development of immune defenses in animals. Read more »
Functional and structural characterization of AntR, an Sb(III) responsive transcriptional repressor
Antimony is considered a priority environmental pollutant by the EPA. The ant operon of the antimony-mining bacterium, C. testosterone, confers resistance to Sb(III). The operon is regulated by the product of the first gene in the operon, antR. This is the first report of the structure and binding properties of antR, with high selectivity for environmental antimony. Read more »
Sifting through Fragments for COVID-19 Treatments
COVID-19 vaccines are essential for preventing serious disease, but the identification of new drugs is still necessary for the treatment of patients who become sick as a result of SARS-CoV-2 infection. Here, scientists used computational docking and crystallography to screen large numbers of small molecules for potential use in drug compounds. Read more »
Scientist at Berkeley Lab Played a Hand in “Inescapable” COVID-19 Antibody Discovery
An antibody therapy that appears to neutralize all known SARS-CoV-2 strains—including newly emerged mutants that can now “escape” from previous antibody therapies—was developed with a little help from structural biologist Jay Nix. His work helped generate detailed structural maps of how antibodies bind to the spike protein, enabling the selection of promising contenders. Read more »
Researchers Set Sights on Another COVID-19 Target
Early in the COVID-19 pandemic, it was quickly established that the receptor binding domain (RBD) of the SARS-CoV-2 spike protein is a prime target for neutralizing antibodies. Now, scientists have found a second region of the spike protein that is targeted by dozens of antibodies, some of which exhibit ultrapotent neutralizing activity. Read more »
Structure of blood coagulation factor VIII in complex with an anti–C1 domain pathogenic antibody inhibitor
van der Waals sphere representation of the factor VIII C1 domain, highlighting surface‐exposed hemophilia A–associated mutations that cause impaired von Willebrand factor binding and overlap with a pathogenic anti‐C1 domain inhibitor epitope. Read more »
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