Stanford Synchrotron Radiation Lightsource

Celiac disease is an autoimmune disorder where the body's immune system attacks its own tissues when gluten is consumed. At the heart of this reaction is an enzyme called Transglutaminase 2 (TG2). TG2 helps modify gluten proteins in a way that makes them more likely to trigger this harmful immune response. This process depends on calcium, but until now, scientists had not fully understood how calcium interacts with TG2.

Olgotrelvir (STI-1558) is a novel antiviral drug designed to address the challenges posed by the emergence of new, more infectious and virulent SARS-CoV-2 variants. This drug is particularly important for populations at risk who may not benefit from existing treatments like Paxlovid due to potential drug-drug interactions. Olgotrelvir exhibits strong antiviral activity against the SARS-CoV-2 main protease (M^pro), including its variants which showed resistant to Paxlovid. Furthermore, it inhibits human cathepsin L (CTSL), a host enzyme critical for viral entry through the endosomal pathway, thereby blocking both the entry and replication of the virus. Phase 1 clinical trials have demonstrated that oral administration of Olgotrelvir achieves effective plasma levels with limited mild adverse effects and a promising reduction in viral RNA load.

In the Wood-Ljungdahl pathway (WLP), nature has devised one of the most elegant methods for the chemical transformation of carbon.¹ The WLP is ancient, present in the last universal common ancestor to life on earth and is the only carbon fixation pathway known to produce more energy than is consumed in terms of net ATP. The WLP functions to scrub our atmosphere of the key greenhouse gas CO₂, utilizing the carbon for energy and for the creation of cellular building material. This process occurs within the context of a large multi-unit protein complex made of carbon monoxide dehydrogenase (CODH) and acetyl-CoA synthase (ACS) in conjunction with a separate corrinoid iron-sulfur protein (CFeSP), which donates a methyl group to the ACS active site, resulting in the formation of acetate in the form of acetyl-CoA from the original CO₂ molecule.

The omicron variant of COVID-19 was identified in the fall of 2021. It stood out from all of the other variants because of the many mutations that simultaneously occurred in its spike protein¹. So far, surveillance and bioinformatics have been the main scientific tools in tracking COVID-19 evolution. Eventually, however, understanding COVID-19 evolution comes down to understanding the functions of key viral mutations. This is where structural biology kicks in and plays a critical role in tracking COVID-19 evolution.