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Science 29 August 1997:
Vol. 277. no. 5330, pp. 1310 - 1313
DOI: 10.1126/science.277.5330.1310

Reports

Induced alpha  Helix in the VP16 Activation Domain upon Binding to a Human TAF

Motonari Uesugi, Origène Nyanguile, Hua Lu, Arnold J. Levine, Gregory L. Verdine *

Activation domains are functional modules that enable sequence-specific DNA binding proteins to stimulate transcription. The structural basis for the function of activation domains is poorly understood. A combination of nuclear magnetic resonance (NMR) and biochemical experiments revealed that the minimal acidic activation domain of the herpes simplex virus VP16 protein undergoes an induced transition from random coil to alpha  helix upon binding to its target protein, hTAFII31 (a human TFIID TATA box-binding protein-associated factor). Identification of the two hydrophobic residues that make nonpolar contacts suggests a general recognition motif of acidic activation domains for hTAFII31.

M. Uesugi, O. Nyanguile, G. L. Verdine, Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.
H. Lu and A. J. Levine, Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
*   To whom correspondence should be addressed.


Volume 277, Number 5330, Issue of 29 August 1997, pp. 1310-1313
©1997 by The American Association for the Advancement of Science.

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