Crystal structure of acetylcholine-binding protein from Bulinus truncatus reveals the conserved structural scaffold and sites of variation in nicotinic acetylcholine receptors

Journal of Biological Chemistry

Volumn 280, Issue 28, 2005, Pages 26457-26466

  Celie, Patrick H N ^a   Klaassen, Remco V ^b   Van Rossum Fikkert, Sarah E ^a   Van Elk, René ^b   Van Nierop, Pim ^b   Smit, August B ^b   Sixma, Titia K ^a  

^a NETHERLANDS CANCER INSTITUTE   (Netherlands)

^b VU UNIVERSITY AMSTERDAM   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; DRUG DOSAGE; POLYMERIC MEMBRANES; PROTEINS;

ACETYLCHOLINE-BINDING PROTEIN (ACHBP); ION CHANNEL FAMILY; ION CHANNEL RECEPTORS; LIGAND BINDING;

CRYSTAL STRUCTURE;

4 AMINOBUTYRIC ACID A RECEPTOR; 4 AMINOBUTYRIC ACID C RECEPTOR; ACETYLCHOLINE; ACETYLCHOLINE BINDING PROTEIN; BINDING PROTEIN; GLYCINE RECEPTOR; ION CHANNEL; NICOTINIC RECEPTOR; SEROTONIN RECEPTOR; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; BINDING SITE; BULINUS; BULINUS TRUNCATUS; CHANNEL GATING; CRYSTAL STRUCTURE; DRUG DESIGN; LIGAND BINDING; LIGAND BINDING DOMAIN; LIGAND GATED ION CHANNEL; LYMNAEA; LYMNAEA STAGNALIS; MODEL; MOLLUSC; MUTATIONAL ANALYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PHARMACOLOGY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN POLYMORPHISM; PROTEIN STABILITY; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; SIGNAL TRANSDUCTION; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; BUNGAROTOXINS; CALORIMETRY; CARRIER PROTEINS; CIRCULAR DICHROISM; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; DRUG DESIGN; IN SITU HYBRIDIZATION; IONS; LIGANDS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLLUSCA; PHYLOGENY; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, CHOLINERGIC; RECEPTORS, NICOTINIC; SEQUENCE HOMOLOGY, AMINO ACID; SIGNAL TRANSDUCTION; TEMPERATURE;

BULINUS TRUNCATUS; LYMNAEA STAGNALIS;

EID: 22144466847     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M414476200     Document Type: Article

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