2e4w | pdb_00002e4w

Crystal structure of the extracellular region of the group II metabotropic glutamate receptor complexed with 1S,3S-ACPD

spinqualitylabelsall models 2e4w, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2e4w is a 2 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: C5A, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GRM3_RAT G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling inhibits adenylate cyclase activity. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structures of the extracellular regions of the group II/III metabotropic glutamate receptors.,Muto T, Tsuchiya D, Morikawa K, Jingami H Proc Natl Acad Sci U S A. 2007 Mar 6;104(10):3759-64. Epub 2007 Feb 26. PMID:17360426 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Metabotropic glutamate receptor 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA