Protein structure with the newly identified switch between a cysteine and lysine residue showing its structure and electron density. This discovery has wide-reaching implications for understanding and treating diseases. Photo: K Tittmann
Protein structure with the newly identified switch between a cysteine and lysine residue showing its structure and electron density. This discovery has wide-reaching implications for understanding and treating diseases. Photo: K Tittmann A research team led by Göttingen University find novel switch in proteins with wide-ranging implications for medical treatments Proteins perform a vast array of functions in the cell of every living organism with critical roles in almost every biological process. Not only do they run our metabolism, manage cellular signaling and are in charge of energy production, as antibodies they are also the frontline workers of our immune system fighting human pathogens like the coronavirus. In view of these important duties, it is not surprising that the activity of proteins is tightly controlled. There are numerous chemical switches that control the structure and, therefore, the function of proteins in response to changing environmental conditions and stress. The biochemical structures and modes of operation of these switches were thought to be well understood.
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