This review summarizes structural studies on kainate receptors that explain unique functional properties of this receptor family. A large number of structures have been solved for ligand binding domain dimer assemblies, giving insight into the subtype selective pharmacology of agonists, antagonists, and allosteric modulators. Structures and biochemical studies on the amino terminal domain reveal mechanisms that play a key role in assembly of heteromeric receptors. Surprisingly, structures of full length homomeric GluK2, GluK3 and heteromeric GluK2/GluK5, receptors reveal a novel structure for the desensitized state that is strikingly different from that for AMPA receptors. This article is part of the Neuropharmacology Special Issue on ‘Glutamate Receptors – Kainate receptors’. •The structure of kainate receptors is reviewed and related to their unique functional properties.•Crystal structures for ligand binding domains reveal subtype specific features and sites for allosteric modulation.•Cryo-EM structures for full length receptors reveal a unique conformation for the desensitized state.