Abstract
The review focuses on chloride-binding structures in the proteins of bacteria, plants, viruses and animals. The structure and amino acid composition of the chloride-binding site and its role in the functioning of structural, regulatory, transport, receptor, channel proteins, transcription factors and enzymes are considered. Data on the important role of chloride-binding structures and chloride anions in the polymerization of fibrin are presented.
Highlights
Among the many ions present in cells and extracellular fluids, the chloride anion is very important
Perhaps electrostatic interactions increase in a hydrophobic slit on albumin molecule
It has been shown in experiments with the acetylating agent methyl acetyl phosphate that the ability of hemoglobin to bind chloride anions depends on its conformational state
Summary
The structure and amino acid composition of the chloride-binding site and its role in the functioning of structural, regulatory, transport, receptor, channel proteins, transcription factors and enzymes are considered. Data on the important role of chloride-binding structures and chloride anions in the polymerization of fibrin are presented. Most chloride anions are not bound, yet some bind to proteins and influence their spatial structure and its transformations [2]. We will review the main groups of proteins that bind chloride anions, their chlorine binding sites, and the similarities they share. Chlorine-binding proteins are functionally and structurally very diverse. They include transcription factors, enzymes (such as blood coagulation system proteins and kinases), Cl- transporters and Cl- channels, receptors, respiration chain complexes, photosynthetic complexes, hemoglobin and albumin, structural proteins, messengers
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