Solution Structure of MSL2 CXC Domain Reveals an Unusual Zn3Cys9 Cluster and Similarity to Pre-SET Domains of Histone Lysine Methyltransferases

PLoS ONE

Volumn 7, Issue 9, 2012, Pages

  Zheng, Sanduo ^a,b   Wang, Jia ^a,b   Feng, Yingang ^c,d   Wang, Jinfeng ^d   Ye, Keqiong ^b  

^a BEIJING NORMAL UNIVERSITY   (China)

^b NATIONAL INSTITUTE OF BIOLOGICAL SCIENCES   (China)

^c QINGDAO INSTITUTE OF BIOENERGY AND BIOPROCESS TECHNOLOGY   (China)

^d INSTITUTE OF BIOPHYSICS   (China)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; HISTONE LYSINE METHYLTRANSFERASE; MSL1 PROTEIN; MSL2 PROTEIN; PROTEIN; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG; ZINC;

ARTICLE; BINDING AFFINITY; BINDING SITE; CIRCULAR DICHROISM; DNA BINDING CYSTEINE RICH CXC DOMAIN; DROSOPHILA; GENE EXPRESSION REGULATION; GENETIC TRANSCRIPTION; MALE; MOLECULAR EVOLUTION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; STRUCTURAL HOMOLOGY; STRUCTURE ANALYSIS; X CHROMOSOME; X CHROMOSOME LINKAGE;

ANIMALS; DNA-BINDING PROTEINS; DROSOPHILA PROTEINS; HISTONE-LYSINE N-METHYLTRANSFERASE; MAGNETIC RESONANCE SPECTROSCOPY; MALE; NUCLEAR PROTEINS; PROTEIN BINDING; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; STRUCTURAL HOMOLOGY, PROTEIN; TRANSCRIPTION FACTORS; ZINC;

EID: 84866676317     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0045437     Document Type: Article

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