English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Significance Glutamate receptor-like (GLR) channels are plant homologs of glutamate receptors in vertebrate synapses; they are calcium-permeable channels involved in root and pollen tube growth, stomatal regulation, and wound signaling. This study presents crystal structures of a plant GLR ligand-binding domain (LBD) in complex with 4 different amino acid ligands and identifies the protein residues responsible for amino acid binding. Binding assays show that the amino acids that trigger GLR-mediated calcium influx inArabidopsis thaliana root tip cells bind the GLR LBD with micromolar affinities.

The structural bases for agonist diversity in an Arabidopsis thaliana glutamate receptor-like channel