ArticleProtein science : a publication of the Protein Society2000
Three-dimensional model of the extracellular domain of the type 4a metabotropic glutamate receptor: new insights into the activation process.
Article in Protein science : a publication of the Protein Society, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
11 citing papers in PubMed, 59 citations in OpenAlex.
- In Silico Studies Targeting G-protein Coupled Receptors for Drug Research Against Parkinson's Disease.Current neuropharmacology · 2018Article
- Ctr9, a Protein in the Transcription Complex Paf1, Regulates Dopamine Transporter Activity at the Plasma Membrane.The Journal of biological chemistry · 2015Article
- Masked selection: a straightforward and flexible approach for the selection of binders against specific epitopes and differentially expressed proteins by phage display.Molecular & cellular proteomics : MCP · 2014Article
- Allosteric modulation of metabotropic glutamate receptors: structural insights and therapeutic potential.Neuropharmacology · 2011Review
- Allosteric modulation of metabotropic glutamate receptors.Advances in pharmacology (San Diego, Calif.) · 2011Review
- Molecular determinants of ligand selectivity in a vertebrate odorant receptor.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2004Article
- No ligand binding in the GB2 subunit of the GABA(B) receptor is required for activation and allosteric interaction between the subunits.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2002Article
- Closure of the Venus flytrap module of mGlu8 receptor and the activation process: Insights from mutations converting antagonists into agonists.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- A single subunit (GB2) is required for G-protein activation by the heterodimeric GABA(B) receptor.The Journal of biological chemistry · 2002Article
- BAY36-7620: a potent non-competitive mGlu1 receptor antagonist with inverse agonist activity.Molecular pharmacology · 2001Article
- Allosteric interactions between GB1 and GB2 subunits are required for optimal GABA(B) receptor function.The EMBO journal · 2001Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Metabotropic glutamate receptors (mGluRs) belong to the family 3 of G-protein-coupled receptors. On these proteins, agonist binding on the extracellular domain leads to conformational changes in the 7-transmembrane domains required for G-protein activation. To elucidate the structural features that might be responsible for such an activation mechanism, we have generated models of the amino terminal domain (ATD) of type 4 mGluR (mGlu4R). The fold recognition search allowed the identification of three hits with a low sequence identity, but with high secondary structure conservation: leucine isoleucine valine-binding protein (LIVBP) and leucine-binding protein (LBP) as already known, and acetamide-binding protein (AmiC). These proteins are characterized by a bilobate structure in an open state for LIVBP/LBP and a closed state for AmiC, with ligand binding in the cleft. Models for both open and closed forms of mGlu4R ATD have been generated. ACPT-I (1-aminocyclopentane 1,3,4-tricarboxylic acid), a selective agonist, has been docked in the two models. In the open form, ACPT-I is only bound to lobe I through interactions with Lys74, Arg78, Ser159, and Thr182. In the closed form, ACPT-I is trapped between both lobes with additional binding to Tyr230, Asp312, Ser313, and Lys317 from lobe II. These results support the hypothesis that mGluR agonists bind a closed form of the ATDs, suggesting that such a conformation of the binding domain corresponds to the active conformation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.