Structure and function of glutamate receptor amino terminal domains

Furukawa, H. (2012) Structure and function of glutamate receptor amino terminal domains. Journal of Physiology, 590 (1). pp. 63-72. ISSN 00223751 (ISSN)

URL: http://www.ncbi.nlm.nih.gov/pubmed/22106178
DOI: 10.1113/jphysiol.2011.213850

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
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 Deposited: 30 Jan 2013 21:40
Last Modified: 03 Apr 2015 20:03
PMCID: PMC3300046
Related URLs:
URI: http://repository.cshl.edu/id/eprint/26944

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