Induced alpha helix in the VP16 activation domain upon binding to a human TAF.
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.
Uesugi
M
M
Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.
Nyanguile
O
O
Lu
H
H
Levine
A J
AJ
Verdine
G L
GL
D000595:Amino Acid Sequence; D017405:Herpes Simplex Virus Protein Vmw65 / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017384:Sequence Deletion; D035381:TATA-Binding Protein Associated Factors; D015534:Trans-Activators / Q000737:chemistry / Q000378:metabolism*; D035362:Transcription Factor TFIID; D015533:Transcriptional Activation
D017405:Herpes Simplex Virus Protein Vmw65; C106849:TAF9 protein, human; D035381:TATA-Binding Protein Associated Factors; D015534:Trans-Activators; D035362:Transcription Factor TFIID