Structure and mechanism of glutamate receptor ion channel assembly, activation and modulation

Structure and mechanism of glutamate receptor ion channel assembly, activation and modulation

Graphical abstract Research highlights ► Analysis of glutamate receptor structure is becoming increasingly sophisticated. ► Novel features include symmetry mismatch and a dimer of dimers assembly. ► Dimer formation is a key mechanism in AMPA receptor biogenesis. ► In NMDA receptors the amino termina...

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Veröffentlicht in:Current opinion in neurobiology 2011-04, Vol.21 (2), p.283-290
1. Verfasser: Mayer, Mark L
Format: Artikel
Sprache:eng
Schlagworte:
alpha -Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors
Animals
Brain
Channel gating
Crystal structure
Data processing
Glutamic acid receptors
Glutamic acid receptors (ionotropic)
Humans
Ion channels
Nervous system
Neurology
Protein Structure, Quaternary
Psychiatry
Receptors, Glutamate - chemistry
Receptors, Glutamate - physiology
Receptors, Glutamate - ultrastructure
Reviews
Synaptic transmission
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Beschreibung
Zusammenfassung:Graphical abstract Research highlights ► Analysis of glutamate receptor structure is becoming increasingly sophisticated. ► Novel features include symmetry mismatch and a dimer of dimers assembly. ► Dimer formation is a key mechanism in AMPA receptor biogenesis. ► In NMDA receptors the amino terminal domain acts as an endogenous regulator. ► NMR data and molecular dynamics simulations give insights into receptor energetics. ► Auxiliary subunits are now key targets for structural and mechanistic analysis.
ISSN:0959-4388
1873-6882
DOI:10.1016/j.conb.2011.02.001