Open AccessAmino acid sensor conserved from bacteria to humans
Author(s) -
Vadim M. Gumerov,
Ekaterina P. Andrianova,
Miguel A. Matilla,
Karen M. Page,
Elizabet MonteagudoCascales,
Annette C. Dolphin,
Tino Krell,
Igor B. Zhulin
Publication year - 2022
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2110415119
Subject(s) - amino acid , receptor , structural motif , biology , biochemistry , bacteria , motif (music) , amino acid residue , computational biology , peptide sequence , microbiology and biotechnology , chemistry , genetics , gene , physics , acoustics
Significance Amino acids are the building blocks of life and important signaling molecules. Despite their common structure, no universal mechanism for amino acid recognition by cellular receptors is currently known. We discovered a simple motif, which binds amino acids in various receptor proteins from all major life-forms. In humans, this motif is found in subunits of calcium channels that are implicated in pain and neurodevelopmental disorders. Our findings suggest that γ-aminobutyric acid–derived drugs bind to the same motif in human proteins that binds natural ligands in bacterial receptors, thus enabling future improvement of important drugs.