Download MendeleyCrystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16.
Liu, Y., Gong, W., Huang, C.C., Herr, W., Cheng, X.(1999) Genes Dev 13: 1692-1703
- PubMed: 10398682
- DOI: https://doi.org/10.1101/gad.13.13.1692
- Primary Citation of Related Structures:
16VP - PubMed Abstract:
On infection, the herpes simplex virus (HSV) virion protein VP16 (Vmw65; alphaTIF) forms a transcriptional regulatory complex-the VP16-induced complex-with two cellular proteins, HCF and Oct-1, on VP16-responsive cis-regulatory elements in HSV immediate-early promoters called TAATGARAT. Comparison of different HSV VP16 sequences reveals a conserved core region that is sufficient for VP16-induced complex formation. The crystal structure of the VP16 core has been determined at 2.1 A resolution. The results reveal a novel, seat-like protein structure. Together with the activity of mutant VP16 proteins, the structure of free VP16 suggests that it contains (1) a disordered carboxy-terminal region that associates with HCF, Oct-1, and DNA in the VP16-induced complex, and (2) a structured region involved in virion assembly and possessing a novel DNA-binding surface that differentiates among TAATGARAT VP16-response elements.
Organizational Affiliation:
Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724, USA.
