Role of two strictly conserved residues in nucleotide flipping and N-glycosylic bond cleavage by human thymine DNA glycosylase

Journal of Biological Chemistry

Volumn 284, Issue 52, 2009, Pages 36680-36688

  Maiti, Atanu ^a   Morgan, Michael T ^a   Drohat, Alexander C ^a  

^a UNIVERSITY OF MARYLAND SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BASE EXCISION REPAIRS; BOND CLEAVAGES; CONSERVED RESIDUES; DEOXYURIDINE; DNA GLYCOSYLASE; DNA PRODUCTS; GENOMIC INTEGRITY; METHYLCYTOSINE; MINOR GROOVES; PRODUCT RELEASE; SUBSTRATE BINDING; TRANSITION STATE; WILD TYPES;

CHEMICAL BONDS; CRYSTAL STRUCTURE; DNA; GENES; NUCLEOTIDES;

SUBSTRATES;

ARGININE; ASPARAGINE; GLYCOSYLATED PROTEIN; THYMINE DNA GLYCOSYLASE;

AMINO ACID SUBSTITUTION; ARTICLE; BASE PAIRING; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; DNA BINDING; DNA CLEAVAGE; ENZYME SPECIFICITY; EXCISION REPAIR; HUMAN; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN FUNCTION; SITE DIRECTED MUTAGENESIS;

AMINO ACID SUBSTITUTION; BINDING SITES; DNA; HUMANS; MUTATION, MISSENSE; NUCLEOTIDES; PROTEIN STRUCTURE, SECONDARY; THYMINE DNA GLYCOSYLASE;

EID: 73649103725     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.062356     Document Type: Article

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