The macro domain is an ADP-ribose binding module

EMBO Journal

Volumn 24, Issue 11, 2005, Pages 1911-1920

  Karras, Georgios I ^a,c   Kustatscher, Georg ^a   Buhecha, Heeran R ^a,b,d   Allen, Mark D ^b   Pugieux, Céline ^a   Sait, Fiona ^b   Bycroft, Mark ^b   Ladurner, Andreas G ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

^c MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^d Trinity Hall ^*  (United Kingdom)

Author keywords

Ligand; Metabolites; NAD; PARP; Protein module

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; POLY(ADENOSINE DIPHOSPHATE RIBOSE);

ARTICLE; CHEMICAL ANALYSIS; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROCESSING; PROTEIN TERTIARY STRUCTURE; STRUCTURE ANALYSIS;

ADENOSINE DIPHOSPHATE; ADENOSINE DIPHOSPHATE RIBOSE; AMINO ACID SEQUENCE; ARCHAEAL PROTEINS; ARCHAEOGLOBUS FULGIDUS; BINDING SITES; CALORIMETRY, DIFFERENTIAL SCANNING; CARRIER PROTEINS; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; HISTONES; HUMANS; HYDROLYSIS; LIGANDS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NEOPLASM PROTEINS; PHOSPHORIC MONOESTER HYDROLASES; POLY ADENOSINE DIPHOSPHATE RIBOSE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SPECIES SPECIFICITY; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 21244444665     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.emboj.7600664     Document Type: Article

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