Versatility in phospho-dependent molecular recognition of the XRCC1 and XRCC4 DNA-damage scaffolds by aprataxin-family FHA domains

DNA Repair

Volumn 35, Issue , 2015, Pages 116-125

  Cherry, Amy L ^a,c   Nott, Timothy J ^a,d   Kelly, Geoffrey ^b   Rulten, Stuart L ^b   Caldecott, Keith W ^b   Smerdon, Stephen J ^a  

^a THE FRANCIS CRICK INSTITUTE   (United Kingdom)

^b UNIVERSITY OF SUSSEX   (United Kingdom)

^c UNIVERSITY OF WORCESTER   (United Kingdom)

^d UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

DNA break repair; DNA damage signalling; FHA domain

Indexed keywords

APRATAXIN; APRATAXIN AND PNKP LIKE FACTOR; CASEIN KINASE II; POLYNUCLEOTIDE KINASE PHOSPHATASE; PROTEIN; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG; XRCC1 PROTEIN; XRCC4 PROTEIN; APLF PROTEIN, HUMAN; APTX PROTEIN, HUMAN; DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; DNA BINDING PROTEIN; DNA LIGASE; NUCLEAR PROTEIN; PHOSPHOTRANSFERASE; PNKP PROTEIN, HUMAN; X-RAY REPAIR CROSS COMPLEMENTING PROTEIN 1; XRCC4 PROTEIN, HUMAN;

ARTICLE; BINDING AFFINITY; BINDING SITE; BIOCHEMICAL ANALYSIS; COMPLEX FORMATION; CRYSTAL STRUCTURE; DNA DAMAGE; DNA REPAIR; FORKHEAD ASSOCIATED DOMAIN; HUMAN; MOLECULAR RECOGNITION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; X RAY CRYSTALLOGRAPHY; X RAY DIFFRACTION; AMINO ACID SEQUENCE; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE; PHOSPHORYLATION; PROTEIN TERTIARY STRUCTURE; ULTRASTRUCTURE;

AMINO ACID SEQUENCE; BINDING SITES; CASEIN KINASE II; CRYSTALLOGRAPHY, X-RAY; DNA DAMAGE; DNA REPAIR; DNA REPAIR ENZYMES; DNA-(APURINIC OR APYRIMIDINIC SITE) LYASE; DNA-BINDING PROTEINS; HUMANS; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; NUCLEAR PROTEINS; PHOSPHORYLATION; PHOSPHOTRANSFERASES (ALCOHOL GROUP ACCEPTOR); PROTEIN STRUCTURE, TERTIARY;

EID: 84945121524     PISSN: 15687864     EISSN: 15687856     Source Type: Journal    
DOI: 10.1016/j.dnarep.2015.10.002     Document Type: Article

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