{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Harms JE"],"funding":["NIA NIH HHS","NIMH NIH HHS","NINDS NIH HHS","National Institutes of Health"],"pagination":["10702-10714"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4036187"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["289(15)"],"pubmed_abstract":["AMPA receptors are gated through binding of glutamate to a solvent-accessible ligand-binding domain. Upon glutamate binding, these receptors undergo a series of conformational rearrangements regulating channel function. Allosteric modulators can bind within a pocket adjacent to the ligand-binding domain to stabilize specific conformations and prevent desensitization. Yelshansky et al. (Yelshansky, M. V., Sobolevsky, A. I., Jatzke, C., and Wollmuth, L. P. (2004) J. Neurosci. 24, 4728-4736) described a model of an electrostatic interaction between the ligand-binding domain and linker region to the pore that regulated channel desensitization. To test this hypothesis, we have conducted a series of experiments focusing on the R628E mutation. Using ultrafast perfusion with voltage clamp, we appl"],"journal":["The Journal of biological chemistry"],"pubmed_title":["A charge-inverting mutation in the \"linker\" region of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors alters agonist binding and gating kinetics independently of allosteric modulators."],"pmcid":["PMC4036187"],"funding_grant_id":["S11NS055883","SC1 AG046907","U54NS083932","U54 NS060659","SC1AG046907","U54 NS083932","R01 MH064700","S11 NS055883"],"pubmed_authors":["Benveniste M","Harms JE","Kessler M","Stone LM","Arai AC","Partin KM"],"additional_accession":[]},"is_claimable":false,"name":"A charge-inverting mutation in the \"linker\" region of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors alters agonist binding and gating kinetics independently of allosteric modulators.","description":"AMPA receptors are gated through binding of glutamate to a solvent-accessible ligand-binding domain. Upon glutamate binding, these receptors undergo a series of conformational rearrangements regulating channel function. Allosteric modulators can bind within a pocket adjacent to the ligand-binding domain to stabilize specific conformations and prevent desensitization. Yelshansky et al. (Yelshansky, M. V., Sobolevsky, A. I., Jatzke, C., and Wollmuth, L. P. (2004) J. Neurosci. 24, 4728-4736) described a model of an electrostatic interaction between the ligand-binding domain and linker region to the pore that regulated channel desensitization. To test this hypothesis, we have conducted a series of experiments focusing on the R628E mutation. Using ultrafast perfusion with voltage clamp, we appl","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Apr","modification":"2025-04-19T01:11:23.106Z","creation":"2019-03-27T01:28:58Z"},"accession":"S-EPMC4036187","cross_references":{"pubmed":["24550387"],"doi":["10.1074/jbc.m113.526921","10.1074/jbc.M113.526921"]}}