Asset Details
Do you wish to reserve the book?
Amino acid sensor conserved from bacteria to humans
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Amino acid sensor conserved from bacteria to humans
Do you wish to request the book?
Amino acid sensor conserved from bacteria to humans
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Amino acid sensor conserved from bacteria to humans
2022
Overview
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 γ-aminobutyric acid (GABA), and it is present in all major receptor types. In humans, this motif is found in α2δ-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 α2δ-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.
Publisher
National Academy of Sciences
Subject
/ Archaea
/ Archaeal Proteins - chemistry
/ Archaeal Proteins - metabolism
/ Bacteria
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - metabolism
/ Biophysics and Computational Biology
/ Calcium
/ Calcium channels (voltage-gated)
/ Channels
/ Domains
/ Drugs
/ Humans
/ Ligands
/ Membrane Proteins - chemistry
/ Membrane Proteins - metabolism
/ Neurodevelopmental disorders
/ Pain
/ Proteins
