Structural basis for specific binding of human MPP8 chromodomain to histone H3 methylated at lysine 9

PLoS ONE

Volumn 6, Issue 10, 2011, Pages

  Li, Jing ^a   Li, Zhihong ^b   Ruan, Jianbin ^a   Xu, Chao ^b   Tong, Yufeng ^b   Pan, Patricia W ^b   Tempel, Wolfram ^b   Crombet, Lissete ^b   Min, Jinrong ^b,c   Zang, Jianye ^a  

^a UNIVERSITY OF SCIENCE AND TECHNOLOGY OF CHINA   (China)

^b UNIVERSITY OF TORONTO   (Canada)

^c UNIVERSITY OF TORONTO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; GLUTAMINE; GLYCINE; HETEROCHROMATIN PROTEIN 1; HISTONE H3; LYSINE; M PHASE PHOSPHOPROTEIN 8; METHIONINE; PHOSPHOPROTEIN; POLYCOMB GROUP PROTEIN; THREONINE; TYROSINE; UNCLASSIFIED DRUG; VALINE; DROSOPHILA PROTEIN; HETEROCHROMATIN PROTEIN 1, DROSOPHILA; HISTONE; MPP8 PROTEIN, HUMAN; NONHISTONE PROTEIN; PEPTIDE; REPRESSOR PROTEIN;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; BINDING AFFINITY; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; DIMERIZATION; DISSOCIATION CONSTANT; ELUTION; GEL PERMEATION CHROMATOGRAPHY; GENE CONTROL; GENE EXPRESSION REGULATION; HUMAN; HUMAN CELL; HYDROGEN BOND; MOLECULAR WEIGHT; PROMOTER REGION; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN MOTIF; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; SURFACE PLASMON RESONANCE; X RAY DIFFRACTION; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; METHYLATION; MOLECULAR GENETICS; PROTEIN TERTIARY STRUCTURE; STRUCTURAL HOMOLOGY; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; CHROMOSOMAL PROTEINS, NON-HISTONE; CRYSTALLOGRAPHY, X-RAY; DROSOPHILA PROTEINS; HISTONES; HUMANS; LYSINE; METHYLATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; PHOSPHOPROTEINS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; REPRESSOR PROTEINS; STRUCTURAL HOMOLOGY, PROTEIN; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 80053935982     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0025104     Document Type: Article

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