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

• DOI: 10.1126/science.277.5330.1310
• Publication Date: 2002-07-27T09:37:56Z
• Authors: Motonari Uesugi; Origène Nyanguile; Hua Lu; Arnold J. Levine; Gregory L. Verdine
• Keywords: Helix (gastropod)

Activation domains are functional modules that enable sequence-specific DNA binding proteins to stimulate transcription. The structural basis for the function of activation is poorly understood. A combination nuclear magnetic resonance (NMR) and biochemical experiments revealed minimal acidic domain herpes simplex virus VP16 protein undergoes an induced transition from random coil α helix upon its target protein, hTAF II 31 (a human TFIID TATA box – protein-associated factor). Identification two hydrophobic residues make nonpolar contacts suggests a general recognition motif 31.