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Título: | Amino acid sensor conserved from bacteria to humans |
Autor: | Gumerov, Vadim M.; Andrianova, E.P.; Matilla, Miguel A. CSIC ORCID; Page, K.M.; Monteagudo-Cascales, Elizabet CSIC ORCID; Dolphin, A.C.; Krell, Tino CSIC ORCID; Zhulin, I.B. | Fecha de publicación: | 25-sep-2022 | Citación: | Gordon Research Conference 2022 on Molecular Basis and Applications of Microbial Signal Detection (2022) | Resumen: | Amino acids are the building blocks of life, and they are also recognized as signals by various receptors in bacteria, archaea, and eukaryotes. Despite their common basic structure, no universal mechanism for amino acid recognition is currently known. Here, we show that a subclass of dCache_1 (double domain found in calcium channels and chemotaxis receptors, family 1), a ubiquitous extracellular sensory domain, contains a simple motif, which recognizes the amino and carboxyl groups of amino acid ligands. We found this motif throughout the Tree of Life. In bacteria and archaea, this motif exclusively binds amino acids, including ¿-aminobutyric acid (GABA), and it is present in all major receptor types. In humans, this motif is found in 2-subunits of voltage-gated calcium channels that are implicated in neuropathic pain and neurodevelopmental disorders and in a recently characterized CACHD1 protein. Our findings suggest that GABA-derived drugs bind to the same motif in human 2-subunits that binds natural GABA ligands in bacterial chemoreceptors. The exact location on the target protein and the mechanism of binding may enable future improvements of drugs targeting pain and neurobiological disorders. | Descripción: | Conferencia Invitada presentada en: Gordon Research Conference 2022 on Molecular Basis and Applications of Microbial Signal Detection, Transduction and Response. Ventura, California EEUU, 25-30 sep (2022) | URI: | http://hdl.handle.net/10261/308566 |
Aparece en las colecciones: | (EEZ) Comunicaciones congresos |
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