The structure of the mammalian RNase H2 complex provides insight into RNA·DNA hybrid processing to prevent immune dysfunction

Journal of Biological Chemistry

Volumn 285, Issue 6, 2010, Pages 3617-3624

  Shaban, Nadine M ^a   Harvey, Scott ^a   Perrino, Fred W ^a   Hollis, Thomas ^a  

^a WAKE FOREST SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC RESIDUES; ACTIVE SITE; BIOCHEMICAL ANALYSIS; CRITICAL FUNCTIONS; DNA POLYMERASE; DNA REPLICATIONS; ENZYME COMPLEXES; HYBRID PROCESSING; IMMUNE ACTIVATION; MOLECULAR BASIS; MULTIPLE CELLULAR FUNCTIONS; NUCLEIC ACID METABOLISM; OKAZAKI FRAGMENTS; PROTEIN-PROTEIN INTERACTIONS; RIBONUCLEOTIDES; RNA PRIMERS; SUBSTRATE SPECIFICITY;

BINDING ENERGY; BINDING SITES; BIOMOLECULES; CELL DEATH; COMPLEXATION; DNA; GENES; MAMMALS; METAL IONS; NUCLEIC ACIDS; PROTEINS; RNA;

CRYSTAL STRUCTURE;

METAL ION; RIBONUCLEASE; RIBONUCLEASE H2; RIBONUCLEASE H2A; RIBONUCLEASE H2B; RIBONUCLEASE H2C; UNCLASSIFIED DRUG; DNA; OKAZAKI FRAGMENTS; PROTEIN SUBUNIT; RIBONUCLEASE H; RIBONUCLEASE HII; RNA;

ARTICLE; AUTOIMMUNE DISEASE; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DNA RNA HYBRIDIZATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME STRUCTURE; MOUSE; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN HYDROLYSIS; PROTEIN PROTEIN INTERACTION; ANIMAL; AUTOIMMUNITY; CHEMICAL STRUCTURE; CHEMISTRY; CONFORMATION; DNA REPLICATION; GENETICS; HUMAN; METABOLISM; NUCLEOTIDE SEQUENCE; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

MAMMALIA;

ANIMALS; AUTOIMMUNITY; BASE SEQUENCE; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DNA; DNA REPLICATION; HUMANS; MICE; MODELS, MOLECULAR; MUTATION; NUCLEIC ACID CONFORMATION; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; RIBONUCLEASE H; RNA; SUBSTRATE SPECIFICITY;

EID: 77950466824     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.059048     Document Type: Article

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