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C300105200v1
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Papers In Press, published online ahead of print March 25, 2003
J. Biol. Chem, 10.1074/jbc.C300105200
Submitted on March 11, 2003
Revised on March 24, 2003
Accepted on March 25, 2003

Is the isolated ligand binding domain a good model of the domain in the native receptor?

Dustin Deming, Qing Cheng, and Vasanthi Jayaraman

Integrative Biology/Pharmacology, University of Texas at Houston, Houston, TX 77030

Corresponding Author: vasanthi.jayaraman{at}uth.tmc.edu

Numerous studies have used the atomic level structure of the isolated ligand binding domain of the glutamate receptor to elucidate the agonist induced activation and desenstitization processes in this group of proteins. However, no study has demonstrated the structural equivalence of the isolated ligand binding fragments and the protein in the native receptor. In this report, using visible absorption spectroscopy we show that the electronic environment of the antagonist 6-cyano-7-nitro-2,3-dihydroxyquinoxaline is identical for the isolated protein and the native glutamate receptors expressed in cells. Hence establishing that the local structure of the ligand binding site is the same in the two proteins, and validating the detailed structure – function relationships that have been developed based on a comparison of the structure of the isolated ligand binding domain and electrophysiological consequences in the native receptor.


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