Acetylcholinesterase H and T dimers are associated through the same contact: Mutations at this interface interfere with the C-terminal T peptide, inducing degradation rather than secretion

Journal of Biological Chemistry

Volumn 276, Issue 40, 2001, Pages 37379-37389

  Morel, Nathalie ^a   Leroy, Jacqueline ^a   Ayon, Annick ^a   Massoulié, Jean ^a   Bon, Suzanne ^a  

^a ECOLE NORMALE SUPÉRIEURE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; DIMERIZATION; DIMERS; ENZYMES; INTERFACES (MATERIALS); OLIGOMERS;

OLIGOMERIZATION;

BIOCHEMISTRY;

ACETYLCHOLINESTERASE; ACETYLCHOLINESTERASE C; ACETYLCHOLINESTERASE H; ACETYLCHOLINESTERASE T; AMPHOPHILE; DIMER; GLYCAN; GLYCOSYLPHOSPHATIDYLINOSITOL; MUTANT PROTEIN; OLIGOMER; PROLINE; QN PROTEIN; SECRETORY PROTEIN; TETRAMER; UNCLASSIFIED DRUG; PEPTIDE; POLYSACCHARIDE;

ALPHA HELIX; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; DIMERIZATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME DEGRADATION; ENZYME GLYCOSYLATION; ENZYME RELEASE; ENZYME STABILITY; ENZYME SUBUNIT; ENZYME SYNTHESIS; MUTATION; NONHUMAN; OLIGOMERIZATION; POINT MUTATION; PRIORITY JOURNAL; PROLINE RICH ATTATCHMENT DOMAIN; PROTEIN DOMAIN; THERMOSTABILITY; AMINO ACID SEQUENCE; ANIMAL; CATALYSIS; CHEMICAL STRUCTURE; GENETICS; METABOLISM; MOLECULAR GENETICS; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; RAT; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; TORPEDO;

ANIMALIA; TORPEDO;

ACETYLCHOLINESTERASE; AMINO ACID SEQUENCE; ANIMALS; CATALYSIS; DIMERIZATION; ENZYME STABILITY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PEPTIDES; POLYSACCHARIDES; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RATS; SEQUENCE HOMOLOGY, AMINO ACID; TORPEDO;

EID: 0035813131     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M103192200     Document Type: Article

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