Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors.
Ionotropic glutamate receptors are functionally diverse but have a common architecture, including the 400-residue amino-terminal domain (ATD). We report a 1.8-A resolution crystal structure of human GluR2-ATD. This dimeric structure provides a mechanism for how the ATDs can drive receptor assembly and subtype-restricted composition. Lattice contacts in a 4.1-A resolution crystal form reveal a tetrameric (dimer-dimer) arrangement consistent with previous cellular and cryo-electron microscopic data for full-length AMPA receptors.
Clayton
Amber
A
Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford, UK.
Siebold
Christian
C
Gilbert
Robert J C
RJ
Sutton
Geoffrey C
GC
Harlos
Karl
K
McIlhinney
R A Jeffrey
RA
Jones
E Yvonne
EY
Aricescu
A Radu
AR
D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D018091:Receptors, AMPA / Q000737:chemistry*
D018091:Receptors, AMPA; C104722:glutamate receptor ionotropic, AMPA 2