The Rad50 zinc-hook is a structure joining Mre11 complexes in DNA recombination and repair

Nature

Volumn 418, Issue 6897, 2002, Pages 562-566

  Hopfner, Karl Peter ^a,b   Craig, Lisa ^a   Moncalian, Gabriel ^a   Zinkel, Robert A ^c   Usui, Takehiko ^d   Owen, Barbara A L ^e   Karcher, Annette ^b   Henderson, Brendan ^f   Bodmer, Jean Luc ^a   McMurray, Cynthia T ^e   Carney, James P ^f   Petrini, John H J ^d   Tainer, John A ^a,g  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b UNIVERSITY OF MUNICH   (Germany)

^c UNIVERSITY OF WISCONSIN MADISON   (United States)

^d MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

^e MAYO CLINIC   (United States)

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

^g LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHROMOSOMES; CRYSTAL STRUCTURE; DNA; ELECTRON MICROSCOPY; REPAIR; SUBSTRATES;

MUTATIONS;

GENETIC ENGINEERING;

ADENOSINE TRIPHOSPHATASE; CYSTEINE; DIMER; MRE11 PROTEIN; NUCLEASE; PROTEIN DERIVATIVE; RAD50 PROTEIN; UNCLASSIFIED DRUG; ZINC ION;

BIOCHEMISTRY; DNA;

ARTICLE; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DNA BINDING; DNA RECOMBINATION; DNA REPAIR; GENE DISRUPTION; GENE FUNCTION; GENE MUTATION; GENETIC CONSERVATION; GENETIC RECOMBINATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN STRUCTURE; SISTER CHROMATID;

ADENOSINE TRIPHOSPHATASES; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; DIMERIZATION; DNA REPAIR; DNA-BINDING PROTEINS; ENDODEOXYRIBONUCLEASES; EXODEOXYRIBONUCLEASES; FUNGAL PROTEINS; HUMANS; MICROSCOPY, ELECTRON; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN BINDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; RADIATION TOLERANCE; RECOMBINATION, GENETIC; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; ZINC;

INSERTION SEQUENCES;

EID: 0036682314     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature00922     Document Type: Article

References (30)

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