Structure and histone binding properties of the Vps75-Rtt109 chaperone-lysine acetyltransferase complex

Journal of Biological Chemistry

Volumn 286, Issue 18, 2011, Pages 15625-15629

  Su, Dan ^a   Hu, Qi ^a   Zhou, Hui ^a   Thompson, James R ^a   Xu, Rui Ming ^b   Zhang, Zhiguo ^a   Mer, Georges ^a  

^a MAYO GRADUATE SCHOOL   (United States)

^b INSTITUTE OF BIOPHYSICS   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL TRANSFERASE; ACTIVATION MECHANISMS; BINDING PROPERTIES; CATALYTIC SITES; CRYSTAL FORMS; ENCLOSED SPACES; HISTONE H3; HYDROGEN/DEUTERIUM EXCHANGE; LYSINE RESIDUES; N-TERMINALS; NMR SPECTROSCOPY; TETRAMERS; X-RAY STRUCTURE;

ACETYLATION; BINDING ENERGY; DIMERS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

AMINO ACIDS;

ACYLTRANSFERASE; CHAPERONE; DIMER; HISTONE H3; MONOMER; RTT109 PROTEIN; UNCLASSIFIED DRUG; VPS75 PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DEUTERIUM HYDROGEN EXCHANGE; HISTONE ACETYLATION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN STRUCTURE; STOICHIOMETRY;

ACETYLATION; CRYSTALLOGRAPHY, X-RAY; HISTONE ACETYLTRANSFERASES; HISTONES; MOLECULAR CHAPERONES; MULTIPROTEIN COMPLEXES; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 79955534838     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.C111.220715     Document Type: Article

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