Y. Liu et al., Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16, GENE DEV, 13(13), 1999, pp. 1692-1703
On infection, the herpes simplex virus (HSV) virion protein VP16 (Vmw65; al
pha TIF) forms a transcriptional regulatory complex-the VP16-induced comple
x-with two cellular proteins, HCF and Oct-1, on VP16-responsive cis-regulat
ory elements in HSV immediate-early promoters called TAATGARAT, Comparison
of different HSV VP16 sequences reveals a conserved core region that is suf
ficient for VP16-induced complex formation. The crystal structure of the VP
16 core has been determined at 2.1 Angstrom resolution. The results reveal
a novel, seat-like protein structure. Together with the activity of mutant
VP16 proteins, the structure of Gee VP16 suggests that it contains (1) a di
sordered carboxy-terminal region that associates with HCF, Oct-1, and DNA i
n the VP16-induced complex, and (2) a structured region involved in virion
assembly and possessing a novel DNA-binding surface that differentiates amo
ng TAATGARAT VP16-response elements.