3H5W
Crystal structure of the GluR2-ATD in space group P212121 without solvent
Summary for 3H5W
| Entry DOI | 10.2210/pdb3h5w/pdb |
| Related | 3H5V |
| Descriptor | Glutamate receptor 2 (1 entity in total) |
| Functional Keywords | glutamate receptor, ligand-gated ion channel, synapse, alternative splicing, 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) |
| Cellular location | Cell membrane; Multi-pass membrane protein: P19491 |
| Total number of polymer chains | 2 |
| Total formula weight | 89018.50 |
| 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: 2024-10-09) |
| 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 Cited by 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: 19461580DOI: 10.1038/emboj.2009.140 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.686 Å) |
Structure validation
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