The glycine binding site of the N-methyl-D-aspartate receptor subunit NR1: Identification of novel determinants of co-agonist potentiation in the extracellular M3-M4 loop region

Proceedings of the National Academy of Sciences of the United States of America

Volumn 93, Issue 12, 1996, Pages 6031-6036

  Hirai, Hirokazu ^a   Kirsch, Joachim ^a,b   Laube, Bodo ^a   Betz, Heinrich ^a   Kuhse, Jochen ^a  

^a MAX PLANCK INSTITUTE FOR BRAIN RESEARCH   (Germany)

^b GOETHE UNIVERSITY   (Germany)

Author keywords

bacterial amino acid binding protein; glutamate receptor; site directed mutagenesis; transmembrane topology

Indexed keywords

EPITOPE; GLUTAMATE RECEPTOR; GLYCINE; N METHYL DEXTRO ASPARTIC ACID RECEPTOR;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CELL CULTURE; GENETIC TRANSFECTION; IMMUNOFLUORESCENCE; LIGAND BINDING; MICROSCOPY; OOCYTE; PRIORITY JOURNAL; RECEPTOR AFFINITY; RNA SYNTHESIS; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; CARRIER PROTEINS; EPITOPES; EXCITATORY AMINO ACID ANTAGONISTS; GLYCINE; KYNURENIC ACID; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OLIGOPEPTIDES; PROTEIN CONFORMATION; RECEPTORS, N-METHYL-D-ASPARTATE;

EID: 0029893942     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.93.12.6031     Document Type: Article

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