Solution structure of the catalytic domain of GCN5 histone acetyltransferase bound to coenzyme A

Nature

Volumn 400, Issue 6739, 1999, Pages 86-89

  Lin, Yingxi ^a,b,c   Fletcher, C Mark ^a,b   Zhou, Jianxin ^d   Allis, C David ^d   Wagner, Gerhard ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^c HARVARD UNIVERSITY   (United States)

^d UNIVERSITY OF VIRGINIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COENZYME A; HISTONE ACETYLTRANSFERASE; HISTONE H3; LEUCINE;

ARTICLE; CHEMICAL REACTION; CHEMICAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; ENZYME MECHANISM; MOLECULAR DYNAMICS; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTON NUCLEAR MAGNETIC RESONANCE; REACTION ANALYSIS; SEQUENCE HOMOLOGY; STRUCTURE ANALYSIS;

ACETYLTRANSFERASES; ALANINE; AMINO ACID SEQUENCE; CATALYSIS; CATALYTIC DOMAIN; COENZYME A; HISTONE ACETYLTRANSFERASES; HISTONES; LYSINE; MACROMOLECULAR SUBSTANCES; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE PROTEINS; SOLUTIONS;

TETRAHYMENA;

EID: 0033168497     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/21922     Document Type: Article

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