1MQJ
Crystal structure of the GluR2 ligand binding core (S1S2J) in complex with willardiine at 1.65 angstroms resolution
Summary for 1MQJ
Entry DOI | 10.2210/pdb1mqj/pdb |
Related | 1FTJ 1FTM 1MM6 1MM7 1MQG 1MQH 1MQI |
Descriptor | glutamate receptor 2, ZINC ION, 2-AMINO-3-(2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID, ... (4 entities in total) |
Functional Keywords | ionotropic glutamate receptor, glur2, ligand binding core, s1s2, partial agonist, willardiine, membrane protein |
Biological source | Rattus norvegicus (Norway rat) More |
Cellular location | Cell membrane; Multi-pass membrane protein: p19491 |
Total number of polymer chains | 1 |
Total formula weight | 29486.26 |
Authors | Jin, R.,Banke, T.G.,Mayer, M.L.,Traynelis, S.F.,Gouaux, E. (deposition date: 2002-09-16, release date: 2003-08-05, Last modification date: 2024-11-06) |
Primary citation | Jin, R.,Banke, T.G.,Mayer, M.L.,Traynelis, S.F.,Gouaux, E. Structural basis for partial agonist action at ionotropic glutamate receptors Nat.Neurosci., 6:803-810, 2003 Cited by PubMed Abstract: An unresolved problem in understanding neurotransmitter receptor function concerns the mechanism(s) by which full and partial agonists elicit different amplitude responses at equal receptor occupancy. The widely held view of 'partial agonism' posits that resting and active states of the receptor are in equilibrium, and partial agonists simply do not shift the equilibrium toward the active state as efficaciously as full agonists. Here we report findings from crystallographic and electrophysiological studies of the mechanism of activation of an AMPA-subtype glutamate receptor ion channel. In these experiments, we used 5-substituted willardiines, a series of partial agonists that differ by only a single atom. Our results show that the GluR2 ligand-binding core can adopt a range of ligand-dependent conformational states, which in turn control the open probability of discrete subconductance states of the intact ion channel. Our findings thus provide a structure-based model of partial agonism. PubMed: 12872125DOI: 10.1038/nn1091 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
Download full validation report