Abstract  Ionotropic glutamate receptors (iGluRs) are ligand‐gated ion channels that open their ion‐conducting pores in response to the binding of agonist glutamate. In recent years, significant progress has been achieved in studies of iGluRs by obtaining numerous structures of isolated water soluble ligand binding and amino terminal domains as well as the first full length crystal structure of GluA2 in the closed, antagonist‐bound state. This structural data combined with electrophysiological and fluorescence recordings, biochemical experiments, mutagenesis and molecular dynamics simulations have greatly improved our understanding of iGluR assembly, activation and desensitization processes. This article reviews the recent structural and functional advances in iGluR field and summarizes them in a simplified model of full length iGluR gating.