On the ligand binding profile and desensitization of plant ionotropic glutamate receptor (iGluR)-like channels functioning in MAMP-triggered Ca2+influx
نویسندگان
چکیده
منابع مشابه
Ionotropic glutamate receptor (iGluR)-like channels mediate MAMP-induced calcium influx in Arabidopsis thaliana.
Binding of specific microbial epitopes [MAMPs (microbe-associated molecular patterns)] to PRRs (pattern recognition receptors) and subsequent receptor kinase activation are key steps in plant innate immunity. One of the earliest detectable events after MAMP perception is a rapid and transient rise in cytosolic Ca2+ levels. In plants, knowledge about the signalling events leading to Ca2+ influx ...
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A simple in silico procedure is proposed with a view to predict the agonist or antagonist character of new, AMPA-type Glu receptor channel ligands. Based on the experimental binding domain structures, the orientation of a single Lys residue close to the ligand binding core was found to be diagnostic of ligand-induced conformational changes. Acting as a switch, the position of the Lys residue in...
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High-resolution studies of ionotropic glutamate receptor (iGluR) extracellular domains are beginning to bridge the gap between structure and function. Crystal structures have defined the ligand binding pocket well beyond what was suggested by mutational analysis and homology models alone, providing initial suggestions about the mechanisms of channel gating and desensitization. NMR-derived backb...
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*Biostructural Research Unit, Department of Medicinal Chemistry, and §Department of Pharmacology and Pharmacotherapy, Faculty of Pharmaceutical Sciences, University of Copenhagen, Universitetsparken 2, DK-2100 Copenhagen, Denmark; †Department of Molecular Neurobiology, Lundbeck A/S, Ottiliavej 9, DK-2500 Valby, Denmark; and ‡Department of Pharmacology, Emory University School of Medicine, 1510 ...
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Ionotropic glutamate receptors (GluRs) are ligand-gated membrane channel proteins found in the central neural system that mediate a fast excitatory response of neurons. In this paper, we report theoretical analysis of the ligand-protein interactions in the binding pocket of the S1S2 (ligand binding) domain of the GluR2 receptor in the closed conformation. By utilizing several theoretical method...
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ژورنال
عنوان ژورنال: Plant Signaling & Behavior
سال: 2012
ISSN: 1559-2324
DOI: 10.4161/psb.21761