2WJW

Crystal structure of the human ionotropic glutamate receptor GluR2 ATD region at 1.8 A resolution

Summary for 2WJW

• Entry DOI: 10.2210/pdb2wjw/pdb
• Related: 2WJX
• Descriptor: GLUTAMATE RECEPTOR 2, 2-acetamido-2-deoxy-beta-D-glucopyranose, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: transport protein, postsynaptic cell membrane, glur2, synapse, membrane, receptor, palmitate, synaptic plasticity, alternative splicing, ion transport, cell junction, cell membrane, transmembrane, phosphoprotein, glutamate receptors, polymorphism, glycoprotein, ionic channel, transport, ion channel, rna editing, lipoprotein
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 44187.10

Authors

Clayton, A.,Siebold, C.,Gilbert, R.J.C.,Sutton, G.C.,Harlos, K.,McIlhinney, R.A.J.,Jones, E.Y.,Aricescu, A.R. (deposition date: 2009-06-01, release date: 2009-08-18, Last modification date: 2024-10-16)

Primary citation

Clayton, A.,Siebold, C.,Gilbert, R.J.C.,Sutton, G.C.,Harlos, K.,Mcilhinney, R.A.J.,Jones, E.Y.,Aricescu, A.R.
Crystal Structure of the Glur2 Amino-Terminal Domain Provides Insights Into the Architecture and Assembly of Ionotropic Glutamate Receptors.
J.Mol.Biol., 392:1125-, 2009

PubMed Abstract: 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.

PubMed: 19651138
DOI: 10.1016/J.JMB.2009.07.082

Experimental method

X-RAY DIFFRACTION (1.8 Å)