ArticleProtein science : a publication of the Protein Society1998
Probing the ligand binding domain of the GluR2 receptor by proteolysis and deletion mutagenesis defines domain boundaries and yields a crystallizable construct.
Article in Protein science : a publication of the Protein Society, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed, 84 citations in OpenAlex.
- Rapid and reversible fluorescent probe enables repeated snapshot imaging of AMPA receptors during synaptic plasticity.Science advances · 2025Article
- Chemical labelling for visualizing native AMPA receptors in live neurons.Nature communications · 2017Article
- Molecular dissection of the interaction between the AMPA receptor and cornichon homolog-3.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
- Structure and dynamics of AMPA receptor GluA2 in resting, pre-open, and desensitized states.Cell · 2014Article
- Thermodynamics and mechanism of the interaction of willardiine partial agonists with a glutamate receptor: implications for drug development.Biochemistry · 2014Article
- A conserved mechanism for gating in an ionotropic glutamate receptor.The Journal of biological chemistry · 2013Article
- Detection of disordered regions in globular proteins using ¹³C-detected NMR.Protein science : a publication of the Protein Society · 2012Article
- The loss of an electrostatic contact unique to AMPA receptor ligand binding domain 2 slows channel activation.Biochemistry · 2012Article
- Structural and functional analysis of two new positive allosteric modulators of GluA2 desensitization and deactivation.Molecular pharmacology · 2011Article
- Challenges for and current status of research into positive modulators of AMPA receptors.British journal of pharmacology · 2010Review
- Hydrophobic side chain dynamics of a glutamate receptor ligand binding domain.The Journal of biological chemistry · 2010Article
- Energy transfer ligands of the GluR2 ligand binding core.Biochemistry · 2010Article
- Mechanisms of antagonism of the GluR2 AMPA receptor: structure and dynamics of the complex of two willardiine antagonists with the glutamate binding domain.Biochemistry · 2009Article
- Time-resolved limited proteolysis of mitogen-activated protein kinase-activated protein kinase-2 determined by LC/MS only.Journal of the American Society for Mass Spectrometry · 2008Article
- NMR spectroscopy of the ligand-binding core of ionotropic glutamate receptor 2 bound to 5-substituted willardiine partial agonists.Journal of molecular biology · 2008Article
- Antidepressant interactions with the NMDA NR1-1b subunit.Journal of biophysics (Hindawi Publishing Corporation : Online) · 2008Article
- Differential regulation of ionotropic glutamate receptors.Biophysical journal · 2007Article
- Characterization of a soluble ligand binding domain of the NMDA receptor regulatory subunit NR3A.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006Article
- Crystallization and preliminary X-ray crystallographic analysis of the GluR0 ligand-binding core from Nostoc punctiforme.Acta crystallographica. Section F, Structural biology and crystallization communications · 2005Article
- Structural determinants of agonist-specific kinetics at the ionotropic glutamate receptor 2.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
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4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Ionotropic glutamate receptors constitute an important family of ligand-gated ion channels for which there is little biochemical or structural data. Here we probe the domain structure and boundaries of the ligand binding domain of the AMPA-sensitive GluR2 receptor by limited proteolysis and deletion mutagenesis. To identify the proteolytic fragments, Maldi mass spectrometry and N-terminal amino acid sequencing were employed. Trypsin digestion of HS1S2 (Chen GQ, Gouaux E. 1997. Proc Natl Acad Sci USA 94:13431-13436) in the presence and absence of glutamate showed that the ligand stabilized the S1 and S2 fragments against complete digestion. Using limited proteolysis and multiple sequence alignments of glutamate receptors as guides, nine constructs were made, folded, and screened for ligand binding activity. From this screen, the S1S21 construct proved to be trypsin- and chymotrypsin-resistant, stable to storage at 4 degrees C, and amenable to three-dimensional crystal formation. The HS1S21 variant was readily prepared on a large scale, the His tag was easily removed by trypsin, and crystals were produced that diffracted to beyond 1.5 A resolution. These experiments, for the first time, pave the way to economical overproduction of the ligand binding domains of glutamate receptors and more accurately map the boundaries of the ligand binding domain.
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