Structural dynamics in α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor gating.
Curr Opin Struct Biol
; 87: 102833, 2024 Aug.
Article
in En
| MEDLINE
| ID: mdl-38733862
ABSTRACT
The ionotropic glutamate receptors (iGluRs) are comprised of α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA), N-methyl-d-aspartate receptor, kainate, and delta subtypes and are pivotal in neuronal plasticity. Recent structural studies on AMPA receptors reveal intricate conformational changes during activation and desensitization elucidating the steps from agonist binding to channel opening and desensitization. Additionally, interactions with auxiliary subunits, including transmembrane AMPA-receptor regulatory proteins, germ-cell-specific gene 1-like protein, and cornichon homologs, intricately modulate AMPA receptors. We discuss the recent high-resolution structures of these complexes that unveil stoichiometry, subunit positioning, and differences in specific side-chain interactions that influence these functional modulations.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Receptors, AMPA
Limits:
Animals
/
Humans
Language:
En
Journal:
Curr Opin Struct Biol
/
Curr. opin. struct. biol
/
Current opinion in structural biology
Journal subject:
BIOLOGIA MOLECULAR
Year:
2024
Document type:
Article
Country of publication:
Reino Unido