The structure of NSD1 reveals an autoregulatory mechanism underlying histone H3K36 methylation

Journal of Biological Chemistry

Volumn 286, Issue 10, 2011, Pages 8361-8368

  Qiao, Qi ^a   Li, Yan ^b   Chen, Zhi ^a   Wang, Mingzhu ^a   Reinberg, Danny ^b   Xu, Rui Ming ^a  

^a INSTITUTE OF BIOPHYSICS   (China)

^b NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; CATALYTIC DOMAINS; COMPUTATIONAL DOCKINGS; FREE ACCESS; GENE PRODUCTS; HISTONE H3; INTRINSIC PROPERTY; METHYLTRANSFERASES; MOLECULAR DYNAMICS SIMULATIONS; MOLECULAR MECHANISM; NUCLEOSOMES; PRODUCT SPECIFICITY; S ADENOSYL L METHIONINES; SUBSTRATE SELECTIVITY;

AMINO ACIDS; COMPUTATIONAL CHEMISTRY; GENES;

MOLECULAR DYNAMICS;

HISTONE H3; HISTONE METHYLTRANSFERASE; PROTEIN NSD1; S ADENOSYLMETHIONINE; UNCLASSIFIED DRUG;

ARTICLE; AUTOREGULATION; ENZYME ACTIVE SITE; ENZYME STABILITY; ENZYME STRUCTURE; HISTONE METHYLATION; MOLECULAR DOCKING; MOLECULAR DYNAMICS; MOLECULAR MODEL; NUCLEOSOME; PRIORITY JOURNAL;

COMPUTER SIMULATION; CRYSTALLOGRAPHY, X-RAY; HISTONE-LYSINE N-METHYLTRANSFERASE; HISTONES; HUMANS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; METHYLATION; MODELS, MOLECULAR; NUCLEAR PROTEINS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SOTOS SYNDROME; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 79953151792     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.204115     Document Type: Article

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