Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor

By N. Kunishima, Y. Shimada, Y. Tsuji, Toshihiro Sato, Masaki Yamamoto, T. Kumasaka, S. Nakanishi, H. Jingami, K. Morikawa. Nature, 2000

1,226 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Materials Chemistry, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/63a01b55cf7ccc8033cb73f4c8cd3d1281d60384

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In Cellular and Molecular Neuroscience

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Brian K. Kobilka

Citations in the corpus

G protein coupled receptor structure and activation. (2007, background): “Dimerization is clearly an important mechanism of receptor activation for the glutamate family of GPCRs [8,47], where ligand-induced changes in the dimer interface of the amino terminal ligand binding domain has been demonstrated by crystallography [48,49].”
Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors. (2009, neutral): “This suggests that the domains of the mGluR flytrap have a larger relative mobility, consistent with the conformational changes observed upon ligand binding.(19) D1-based superpositions with open and closed (ligand-bound) LIVBP structures reveal that GluR2-ATD has an intermediate degree of flytrap c”
Ionotropic and metabotropic glutamate receptor structure and pharmacology (2005, neutral): “Functional mGluRs are thought to comprise homodimers stabilised by both an intersubunit disulphide bond and hydrophobic interactions (Romano et al. 1996; Kunishima et al. 2000; Tsuji et al. 2000; Tsuchiya et al. 2002).”
G-Protein-coupled receptor oligomerization and its potential for drug discovery (2002, background): “cgi?l=2911">mGlu 1 metabotropic glutamate receptor has shown that a 'closed–open' conformation of the ligand-binding regions is possible; that is, a conformation in which the ligand-binding domain of one receptor is occupied, whereas the ligand-binding domain of its partner is unoccupie”
The receptors and cells for mammalian taste (2006, background): “, and are characterized by the presence of long amino-terminal extracellular domains that are believed to mediate ligand recognition and bindin”
Glutamate Receptor Ion Channels: Structure, Regulation, and Function (2010, background): “Overall, the GluN2B ATD structure resembles the ligand binding domain of the metabotropic glutamate receptor mGluR1 (Kunishima et al., 2000), although the position of R1 is 50° twisted relative to R2 in GluN2B ATD compared with mGluR1.”
Metabotropic glutamate receptors: From the workbench to the bedside (2010, background): “A number of 3D modeling studies (O’Hara et al., 1993), but most importantly, the resolution of a crystal structure of the mGlu1 extracellular domain (Kunishima et al., 2000; Tsuchiya et al., 2002) confirmed that the glutamate binding domain is structurally similar to LIVBP-like proteins (Fig.”
Functional Selectivity and Classical Concepts of Quantitative Pharmacology (2007, background): “…crystallography studies of the soluble N-terminal binding sites of metabotropic glutamate receptors, agonist binding is thought to alter the relative orientation of the dimer formed by the two extracellular binding domains (Kunishima et al., 2000; Tsuchiya et al., 2002; Kniazeff et al., 2004).”
The receptors for mammalian sweet and umami taste. (2003, background): “Heterolo- tions of the domains essential for glutamate recognition as revealed by the crystal structure of the glutamategous expression studies of rodent T1Rs in HEK cells demonstrated that T1R1 and T1R3 combine to form a binding domain of mGluR (Kunishima et al., 2000).”
Oligomerization of G-protein-coupled transmitter receptors (2001, background): “Indeed, this part of the receptor, constituting its ligand-recognition and binding domain, was found to exist as a dimer whether glutamate was present or not, with the addition of glutamate leading to a significant conformational change of the pre-existing dime”
Heterotrimeric G protein activation by G-protein-coupled receptors (2008, background): “Glutamate family receptors have a 'Venus flytrap' N terminus that is composed of two lobes that close around the ligan”