title: Structure and function of glutamate receptor amino terminal domains.
abstract: The amino terminal domain (ATD) of ionotropic glutamate receptor (iGluR) subunits resides at the extracellular region distal to the membrane. The ATD is structurally and functionally the most divergent region of the iGluR subunits. Structural studies on full-length GluA2 and the ATDs from three iGluR subfamilies have shed light on how the ATD facilitates subunit assembly, accommodates allosteric modulator compounds, and controls gating properties. Here recent developments in structural and functional studies on iGluR ATDs are reviewed.
authors: Cold Spring Harbor Laboratory, WM Keck Structural Biology Laboratory, Cold Spring Harbor, NY 11724, USA. furukawa@cshl.edu
authors: Hiro
authors: H
authors: Furukawa
mesh_terms: D006801:Humans; D008958:Models, Molecular; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary; D058468:Receptors, Ionotropic Glutamate / Q000737:chemistry* / Q000378:metabolism*; D013329:Structure-Activity Relationship
chemical_list: D058468:Receptors, Ionotropic Glutamate