Structural and sequence motifs of protein (histone) methylation enzymes

Annual Review of Biophysics and Biomolecular Structure

Volumn 34, Issue , 2005, Pages 267-294

  Cheng, Xiaodong ^a   Collins, Robert E ^a   Zhang, Xing ^a  

^a EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Protein arginine methyltransferases; Protein lysine methyltransferases; S adenosyl L methionine (AdoMet); SET domain proteins

Indexed keywords

ARGININE; ENZYME; GLUTAMINE; HISTONE; LYSINE;

AMINO ACID SEQUENCE; CHROMATIN STRUCTURE; COVALENT BOND; ENZYME STRUCTURE; GENOME ANALYSIS; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN METHYLATION; PROTEIN MODIFICATION; PROTEIN MOTIF; PROTEOMICS; REGULATORY MECHANISM; REVIEW; TRANSCRIPTION REGULATION;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; ARGININE; BINDING SITES; CHROMATIN; CRYSTALLOGRAPHY, X-RAY; HISTONE-LYSINE N-METHYLTRANSFERASE; HISTONES; HUMANS; LYSINE; MASS SPECTROMETRY; METHYLATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; PHENYLALANINE; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEINS; PROTONS; SEQUENCE HOMOLOGY, AMINO ACID; TYROSINE; ZINC;

EID: 20544461679     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.biophys.34.040204.144452     Document Type: Review

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