3H5V

Crystal structure of the GluR2-ATD

Summary for 3H5V

• Entry DOI: 10.2210/pdb3h5v/pdb
• Related: 3H5W
• Descriptor: Glutamate receptor 2, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: glutamate receptor, ligand-gated ion channel, synapse, cell junction, cell membrane, endoplasmic reticulum, glycoprotein, ion transport, ionic channel, lipoprotein, membrane, palmitate, phosphoprotein, postsynaptic cell membrane, receptor, rna editing, transmembrane, transport, transport protein
• Biological source: Rattus norvegicus (brown rat,rat,rats)
• Total number of polymer chains: 3
• Total formula weight: 134376.55

Authors

Jin, R.,Singh, S.K.,Gu, S.,Furukawa, H.,Sobolevsky, A.,Zhou, J.,Jin, Y.,Gouaux, E. (deposition date: 2009-04-22, release date: 2009-06-09, Last modification date: 2020-07-29)

Primary citation

Jin, R.,Singh, S.K.,Gu, S.,Furukawa, H.,Sobolevsky, A.I.,Zhou, J.,Jin, Y.,Gouaux, E.
Crystal structure and association behaviour of the GluR2 amino-terminal domain.
Embo J., 28:1812-1823, 2009

PubMed Abstract: Fast excitatory neurotransmission is mediated largely by ionotropic glutamate receptors (iGluRs), tetrameric, ligand-gated ion channel proteins comprised of three subfamilies, AMPA, kainate and NMDA receptors, with each subfamily sharing a common, modular-domain architecture. For all receptor subfamilies, active channels are exclusively formed by assemblages of subunits within the same subfamily, a molecular process principally encoded by the amino-terminal domain (ATD). However, the molecular basis by which the ATD guides subfamily-specific receptor assembly is not known. Here we show that AMPA receptor GluR1- and GluR2-ATDs form tightly associated dimers and, by the analysis of crystal structures of the GluR2-ATD, propose mechanisms by which the ATD guides subfamily-specific receptor assembly.

PubMed: 19461580
DOI: 10.1038/emboj.2009.140

Experimental method

X-RAY DIFFRACTION (2.33 Å)