The structure of GABPα/β: An ETS domain-ankyrin repeat heterodimer bound to DNA

Science

Volumn 279, Issue 5353, 1998, Pages 1037-1041

  Batchelor, Adrian H ^a   Piper, Derek E ^a   Charles De La Brousse, Fabienne ^b   McKnight, Steven L ^c   Wolberger, Cynthia ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b AMGEN INC   (United States)

^c UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN; PROTEIN SUBUNIT; DNA; DNA BINDING PROTEIN; GA BINDING PROTEIN; ONCOPROTEIN; PROTO ONCOGENE PROTEIN SPI 1; PROTO-ONCOGENE PROTEIN SPI-1; RECOMBINANT PROTEIN; TRANSACTIVATOR PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR ETS;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; DNA BINDING; GENE EXPRESSION; HYDROGEN BOND; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; TRANSCRIPTION REGULATION; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; DIMERIZATION; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ANKYRINS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; DNA; DNA-BINDING PROTEINS; GA-BINDING PROTEIN TRANSCRIPTION FACTOR; HYDROGEN BONDING; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTO-ONCOGENE PROTEINS; PROTO-ONCOGENE PROTEINS C-ETS; RECOMBINANT PROTEINS; TRANS-ACTIVATORS; TRANSCRIPTION FACTORS;

EID: 0032512459     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.279.5353.1037     Document Type: Article

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38. We thank S. Soisson and E. Reisinger for continuous assistance; S. Prigge, D. Hammontree, and D. Leahy for programs; M. Bianchet and M. Amzel for x-ray room assistance; C. Ogata for beamline assistance; N. Pavletich for 53BP2 coordinates; and B. Graves for Ets-1 samples. This work was initiated during a sabbatical visit by S.L.M. in the laboratory of C.W. At that time S.L.M. was supported by the Carnegie Institute of Washington and the Howard Hughes Medical Institute. A.H.B., D.E.P., and C.W. were supported by the Howard Hughes Medical Institute. C.W. also received support from the David and Lucile Packard Foundation. Coordinates have been deposited at the Brookhaven Protein Data Bank (accession code 1 awc).