Crystal structure of the FTO protein reveals basis for its substrate specificity

Nature

Volumn 464, Issue 7292, 2010, Pages 1205-1209

  Han, Zhifu ^a   Niu, Tianhui ^a,b   Chang, Junbiao ^c   Lei, Xiaoguang ^a,d   Zhao, Mingyan ^a   Wang, Qiang ^c   Cheng, Wei ^a   Wang, Jinjing ^a   Feng, Yi ^a   Chai, Jijie ^a,e  

^a NATIONAL INSTITUTE OF BIOLOGICAL SCIENCES   (China)

^b CHINA AGRICULTURAL UNIVERSITY   (China)

^c ZHENGZHOU UNIVERSITY   (China)

^d TIANJIN UNIVERSITY   (China)

^e TSINGHUA UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

3 METHYLTHYMIDINE; 3 METHYLURACIL; DOUBLE STRANDED DNA; DOUBLE STRANDED RNA; FAT MASS AND OBESITY ASSOCIATED PROTEIN; NUCLEAR PROTEIN; PROTEIN ALKB; THYMIDINE; THYMINE; UNCLASSIFIED DRUG;

CATALYSIS; CRYSTAL STRUCTURE; DNA; GENE; INHIBITOR; OBESITY; PROTEIN; SUBSTRATE;

AMINO TERMINAL SEQUENCE; ARTICLE; BIOCHEMISTRY; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; ENZYME SPECIFICITY; HYDROGEN BOND; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; BIOCATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DNA; DNA, SINGLE-STRANDED; HUMANS; METHYLATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEINS; RNA; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; THYMIDINE; URACIL;

EID: 77951623073     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature08921     Document Type: Article

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