Cryo-EM structures of the triheteromeric NMDA receptor and its allosteric modulation

Science

Volumn 355, Issue 6331, 2017, Pages

  Lü, Wei ^a   Du, Juan ^a   Goehring, April ^a   Gouaux, Eric ^a  

^a OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

N METHYL DEXTRO ASPARTIC ACID RECEPTOR; TRIHETEROMERIC N METHYL DEXTRO ASPARTIC ACID RECEPTOR; UNCLASSIFIED DRUG; GLUTAMATE RECEPTOR; MONOCLONAL ANTIBODY; N-METHYL D-ASPARTATE RECEPTOR SUBTYPE 2A; NR1 PROTEIN, XENOPUS; NR2B NMDA RECEPTOR; XENOPUS PROTEIN;

ANATOMY; CHEMICAL BINDING; COMPARATIVE STUDY; CRYSTAL STRUCTURE; ELECTRON MICROSCOPY; GENETIC ANALYSIS; PROTEIN;

ALLOSTERISM; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CRYOELECTRON MICROSCOPY; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN ISOLATION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; ANIMAL; CHEMISTRY; IMMUNOLOGY; MOLECULAR MODEL; NERVE CELL PLASTICITY; PROTEIN DOMAIN; PROTEIN MULTIMERIZATION; ULTRASTRUCTURE; XENOPUS LAEVIS;

ALLOSTERIC REGULATION; ANIMALS; ANTIBODIES, MONOCLONAL; CRYOELECTRON MICROSCOPY; MODELS, MOLECULAR; NEURONAL PLASTICITY; PROTEIN DOMAINS; PROTEIN MULTIMERIZATION; RECEPTORS, GLUTAMATE; RECEPTORS, N-METHYL-D-ASPARTATE; XENOPUS LAEVIS; XENOPUS PROTEINS;

EID: 85013781123     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aal3729     Document Type: Article

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