1EWV
CRYSTAL STRUCTURE OF METABOTROPIC GLUTAMATE RECEPTOR SUBTYPE 1 LIGAND FREE FORM II
Summary for 1EWV
| Entry DOI | 10.2210/pdb1ewv/pdb |
| Related | 1EWK 1EWT |
| Descriptor | METABOTROPIC GLUTAMATE RECEPTOR SUBTYPE 1 (1 entity in total) |
| Functional Keywords | signal transduction, neurotransmitter, cns, neuron, signaling protein |
| Biological source | Rattus norvegicus (Norway rat) |
| Cellular location | Cell membrane; Multi-pass membrane protein: P23385 |
| Total number of polymer chains | 2 |
| Total formula weight | 110517.41 |
| Authors | Kunishima, N.,Shimada, Y.,Tsuji, Y.,Jingami, H.,Morikawa, K. (deposition date: 2000-04-27, release date: 2000-12-18, Last modification date: 2024-11-20) |
| Primary citation | Kunishima, N.,Shimada, Y.,Tsuji, Y.,Sato, T.,Yamamoto, M.,Kumasaka, T.,Nakanishi, S.,Jingami, H.,Morikawa, K. Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor. Nature, 407:971-977, 2000 Cited by PubMed Abstract: The metabotropic glutamate receptors (mGluRs) are key receptors in the modulation of excitatory synaptic transmission in the central nervous system. Here we have determined three different crystal structures of the extracellular ligand-binding region of mGluR1--in a complex with glutamate and in two unliganded forms. They all showed disulphide-linked homodimers, whose 'active' and 'resting' conformations are modulated through the dimeric interface by a packed alpha-helical structure. The bi-lobed protomer architectures flexibly change their domain arrangements to form an 'open' or 'closed' conformation. The structures imply that glutamate binding stabilizes both the 'active' dimer and the 'closed' protomer in dynamic equilibrium. Movements of the four domains in the dimer are likely to affect the separation of the transmembrane and intracellular regions, and thereby activate the receptor. This scheme in the initial receptor activation could be applied generally to G-protein-coupled neurotransmitter receptors that possess extracellular ligand-binding sites. PubMed: 11069170DOI: 10.1038/35039564 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4 Å) |
Structure validation
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