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Science 29 August 1997: Vol. 277. no. 5330, pp. 1310 - 1313 DOI: 10.1126/science.277.5330.1310
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Reports
Induced 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 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.
Read the Full Text
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