Recovery from desensitization in GluA2 AMPA receptors is affected by a single mutation in the N-terminal domain interface.

Abstract excerpt

AMPA-type ionotropic glutamate receptors (AMPARs) are central to various neurological processes, including memory and learning. They assemble as homo- or heterotetramers of GluA1, GluA2, GluA3, and GluA4 subunits, each consisting of an N-terminal domain (NTD), a ligand-binding domain, a transmembrane domain, and a C-terminal domain. While AMPAR gating is primarily controlled by reconfiguration in the...

Topics

• Humans
• HEK293 Cells
• Ligands
• Molecular Dynamics Simulation
• Mutation
• Protein Domains
• Receptors, AMPA
• Allosteric Regulation