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

EMBO Journal

Volumn 17, Issue 16, 1998, Pages 4704-4711

  Lampinen, Milla ^a,b   Pentikäinen, Olli ^c,d   Johnson, Mark S ^c,d   Keinänen, Kari ^a,b  

^a UNIVERSITY OF HELSINKI   (Finland)

^b VTT TECHNICAL RESEARCH CENTRE OF FINLAND   (Finland)

^c ÅBO AKADEMI UNIVERSITY   (Finland)

^d UNIVERSITY OF TURKU   (Finland)

Author keywords

Glutamate; Ligand binding; Neurotransmission; Quinoxalinedione antagonists; Site directed mutagenesis

Indexed keywords

AMINO ACID; AMPA RECEPTOR; ARGININE; BACTERIAL PROTEIN; BINDING PROTEIN; GLUTAMATE RECEPTOR; GLUTAMINE; RECEPTOR SUBUNIT;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING SITE; CONTROLLED STUDY; ISOTOPE LABELING; LIGAND BINDING; MOLECULAR MODEL; NEUROTRANSMISSION; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; ANIMALS; BACTERIAL PROTEINS; BINDING SITES; CATIONS; CELL LINE; EXCITATORY AMINO ACID ANTAGONISTS; GLUTAMIC ACID; INSECTS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; QUINOXALINES; RECEPTORS, AMPA; RECEPTORS, GLUTAMATE; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

BACTERIA (MICROORGANISMS);

EID: 0032541434     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.16.4704     Document Type: Article

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