Structure and activity of the peptidyl-prolyl isomerase domain from the histone chaperone Fpr4 toward histone H3 proline isomerization

Journal of Biological Chemistry

Volumn 288, Issue 36, 2013, Pages 25826-25837

  Monneau, Yoan R ^a   Soufari, Heddy ^a,b   Nelson, Christopher J ^c   Mackereth, Cameron D ^a,b  

^a INSTITUT EUROPÉEN DE CHIMIE ET BIOLOGIE   (France)

^b UNIVERSITÉ DE BORDEAUX   (France)

^c UNIVERSITY OF VICTORIA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC EFFICIENCIES; FK506-BINDING PROTEINS; HISTONE H3; ISOMERASE ACTIVITY; PEPTIDYL-PROLYL ISOMERASE; PROLINE ISOMERIZATION; STRUCTURE AND ACTIVITIES; SUBSTRATE PEPTIDES;

BIOCHEMISTRY; BIOLOGY;

PROTEINS;

CHAPERONE; CHYMOTRYPSIN; FPR4 PROTEIN; HISTONE H3; PEPTIDYLPROLYL ISOMERASE; PROLINE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CHEMICAL BOND; CONTROLLED STUDY; ENZYME SUBSTRATE; ISOMERIZATION; MOLECULAR RECOGNITION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDYLPROLYL BOND; PRIORITY JOURNAL; PROTEIN DOMAIN; SACCHAROMYCES CEREVISIAE; STRUCTURE ACTIVITY RELATION;

EPIGENETICS; FKBP; HISTONES; NMR; PROLYL ISOMERASE; PROTEIN STRUCTURE;

CATALYSIS; HISTONE CHAPERONES; HISTONES; MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDYLPROLYL ISOMERASE; PROLINE; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; TACROLIMUS BINDING PROTEINS;

EID: 84883719624     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.479964     Document Type: Article

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