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Updated: May 27, 2026

High Precision FRET at Single-molecule Level for Biomolecule Structure Determination
Published on: May 13, 2017
Structure and function of glutamate receptor amino terminal domains
1Cold Spring Harbor Laboratory, WM Keck Structural Biology Laboratory, Cold Spring Harbor, NY 11724, USA. furukawa@cshl.edu
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.
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