2OJT
Structure and mechanism of kainate receptor modulation by anions
Summary for 2OJT
Entry DOI | 10.2210/pdb2ojt/pdb |
Related | 2F34 2F36 |
Descriptor | Glutamate receptor, ionotropic kainate 1, BROMIDE ION, PENTAETHYLENE GLYCOL, ... (5 entities in total) |
Functional Keywords | membrane protein |
Biological source | Rattus norvegicus (Norway rat) More |
Cellular location | Cell membrane; Multi-pass membrane protein: P22756 |
Total number of polymer chains | 2 |
Total formula weight | 59766.13 |
Authors | Mayer, M.L. (deposition date: 2007-01-14, release date: 2007-04-03, Last modification date: 2023-08-30) |
Primary citation | Plested, A.J.,Mayer, M.L. Structure and mechanism of kainate receptor modulation by anions. Neuron, 53:829-841, 2007 Cited by PubMed Abstract: L-glutamate, the major excitatory neurotransmitter in the human brain, activates a family of ligand-gated ion channels, the major subtypes of which are named AMPA, kainate, and NMDA receptors. In common with many signal transduction proteins, glutamate receptors are modulated by ions and small molecules, including Ca(2+), Mg(2+), Zn(2+), protons, polyamines, and steroids. Strikingly, the activation of kainate receptors by glutamate requires the presence of both Na(+) and Cl(-) in the extracellular solution, and in the absence of these ions, receptor activity is abolished. Here, we identify the site and mechanism of action of anions. Surprisingly, we find that Cl(-) ions are essential structural components of kainate receptors. Cl(-) ions bind in a cavity formed at the interface between subunits in a dimer pair. In the absence of Cl(-), dimer stability is reduced, the rate of desensitization increases, and the fraction of receptors competent for activation by glutamate drops precipitously. PubMed: 17359918DOI: 10.1016/j.neuron.2007.02.025 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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