Induced α helix in the VP16 activation domain upon binding to a human TAF

Science

Volumn 277, Issue 5330, 1997, Pages 1310-1313

  Uesugi, Motonari ^a   Nyanguile, Origène ^a   Lu, Hua ^b   Levine, Arnold J ^b   Verdine, Gregory L ^a  

^a HARVARD UNIVERSITY   (United States)

^b PRINCETON UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; TRANSCRIPTION FACTOR; VIRUS PROTEIN;

ALPHA HELIX; ARTICLE; HERPES SIMPLEX VIRUS; HUMAN; MOLECULAR RECOGNITION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN TARGETING; TATA BOX; TRANSACTIVATION;

AMINO ACID SEQUENCE; HERPES SIMPLEX VIRUS PROTEIN VMW65; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SEQUENCE DELETION; TATA-BINDING PROTEIN ASSOCIATED FACTORS; TRANS-ACTIVATION (GENETICS); TRANS-ACTIVATORS; TRANSCRIPTION FACTOR TFIID;

EID: 0030756675     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.277.5330.1310     Document Type: Article

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17. ∥31 has been identified in yeast.
18. ∥31 has been identified in yeast.
19. ∥31 has been identified in yeast.
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46. We thank B. Dynlacht and J. Ross for helpful advice on transcription assays and S. Wolfe and P. Zhou for discussion about the NMR results. Supported in part by a grant from the Hoffman-La Roche Institute of Chemistry and Medicine and an NSF Presidential Young Investigator Award (G.L.V.); the Leukemia Society of America and the Naito Foundation (M.U.); and the Swiss National Foundation of Scientific Research (O.N.). The NMR spectrometer used in this work was purchased with funding from NSF (CHE93-12233).