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

Science  29 Aug 1997:
Vol. 277, Issue 5330, pp. 1310-1313
DOI: 10.1126/science.277.5330.1310

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Abstract

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 α helix upon binding to its target protein, hTAFII31 (a human TFIID TATA boxbinding protein-associated factor). Identification of the two hydrophobic residues that make nonpolar contacts suggests a general recognition motif of acidic activation domains for hTAFII31.

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