2E4V

Crystal structure of the extracellular region of the group II metabotropic glutamate receptor complexed with DCG-IV

Summary for 2E4V

• Entry DOI: 10.2210/pdb2e4v/pdb
• Related: 2E4U 2E4W 2E4X 2E4Y 2E4Z
• Descriptor: Metabotropic glutamate receptor 3, 2-acetamido-2-deoxy-beta-D-glucopyranose, (1R,2R)-3-[(S)-amino(carboxy)methyl]cyclopropane-1,2-dicarboxylic acid, ... (4 entities in total)
• Functional Keywords: g-protein-coupled receptor, neuron, central nerve system, signaling protein
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cell membrane; Multi-pass membrane protein: P31422
• Total number of polymer chains: 2
• Total formula weight: 127083.31

Authors

Muto, T.,Tsuchiya, D.,Morikawa, K.,Jingami, H. (deposition date: 2006-12-17, release date: 2007-02-27, Last modification date: 2024-11-06)

Primary citation

Muto, T.,Tsuchiya, D.,Morikawa, K.,Jingami, H.
Structures of the extracellular regions of the group II/III metabotropic glutamate receptors
Proc.Natl.Acad.Sci.Usa, 104:3759-3764, 2007

PubMed Abstract: Metabotropic glutamate receptors play major roles in the activation of excitatory synapses in the central nerve system. We determined the crystal structure of the entire extracellular region of the group II receptor and that of the ligand-binding region of the group III receptor. A comparison among groups I, II, and III provides the structural basis that could account for the discrimination of group-specific agonists. Furthermore, the structure of group II includes the cysteine-rich domain, which is tightly linked to the ligand-binding domain by a disulfide bridge, suggesting a potential role in transmitting a ligand-induced conformational change into the downstream transmembrane region. The structure also reveals the lateral interaction between the two cysteine-rich domains, which could stimulate clustering of the dimeric receptors on the cell surface. We propose a general activation mechanism of the dimeric receptor coupled with both ligand-binding and interprotomer rearrangements.

PubMed: 17360426
DOI: 10.1073/pnas.0611577104

Experimental method

X-RAY DIFFRACTION (2.4 Å)