Scientists discover fundamental regulation mechanism of proteins
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. So a team of researchers at the University of Göttingen were surprised to discover a completely novel, but until now overlooked, on/off switch that seems to be a ubiquitous regulatory element in
Overlooked Covalent Crosslink an On/Off Switch for Proteins
Protein structure showing a newly identified crosslink, one between a cysteine residue and a lysine residue. (Electron densities are indicated in yellow.) The crosslink has wide-reaching implications for the engineering of proteins, the unraveling of disease mechanisms, and the development of new drugs. [Kai Tittmann University of Göttingen]
May 5, 2021
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Make room, disulfide crosslinks. There’s a new kind of crosslink in proteins. Instead of an S–S bridge connecting two cysteine residues, it consists of an N–O–S bridge between a lysine and a cysteine. (The “N” comes from a lysine residue’s NH
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IMAGE: 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. view more
Credit: K Tittmann
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