Furukawa, H. (February 2012) Structure and function of glutamate receptor amino terminal domains. Journal of Physiology, 590 (1). pp. 63-72. ISSN 00223751 (ISSN)
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. © 2012 The Author. The Journal of Physiology © 2012 The Physiological Society.
Item Type: | Paper |
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Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification organs, tissues, organelles, cell types and functions > cell types and functions > cell functions bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > glutamate receptor bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types |
CSHL Authors: | |
Communities: | CSHL labs > Furukawa lab |
Depositing User: | Matt Covey |
Date: | 14 February 2012 |
Date Deposited: | 30 Jan 2013 21:40 |
Last Modified: | 03 Apr 2015 20:03 |
PMCID: | PMC3300046 |
Related URLs: | |
URI: | https://repository.cshl.edu/id/eprint/26944 |
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