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Structure and function of glutamate receptor amino terminal domains
Author(s) -
Furukawa Hiro
Publication year - 2012
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1113/jphysiol.2011.213850
Subject(s) - ionotropic effect , ionotropic glutamate receptor , allosteric regulation , protein subunit , glutamate receptor , gating , biophysics , extracellular , chemistry , neuroscience , biology , microbiology and biotechnology , biochemistry , receptor , gene
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.