AMPA receptors and bacterial periplasmic amino acid-binding proteins share the ionic mechanism of ligand recognition

In order to identify key structural determinants for ligand recognition, we subjected the ligand‐binding domain of the α‐amino‐3‐hydroxy‐5‐methyl‐4‐isoxazole propionic acid (AMPA)‐selective glutamate receptor GluR‐D subunit to site‐directed mutagenesis. Based on the analysis of the [ 3 H]AMPA‐bindin...

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Veröffentlicht in:	The EMBO journal 1998-08, Vol.17 (16), p.4704-4711
Hauptverfasser:	Lampinen, Milla, Pentikäinen, Olli, Johnson, Mark S., Keinänen, Kari
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Binding Sites Cations Cell Line Excitatory Amino Acid Antagonists - pharmacology glutamate Glutamic Acid - metabolism Insecta ligand binding Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed neurotransmission quinoxalinedione antagonists Quinoxalines - pharmacology Receptors, AMPA - chemistry Receptors, AMPA - genetics Receptors, AMPA - metabolism Receptors, Glutamate - drug effects Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Sequence Homology, Amino Acid site-directed mutagenesis
Online-Zugang:	Volltext
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