Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16
Abstract
On infection, the herpes simplex virus (HSV) virion protein VP16 (Vmw65; αTIF) 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 Å 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.
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Present addresses: 4Department of Biochemistry, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong; 5The Ohio State University, Columbus, Ohio 43210 USA; 6Molecular Neurogenetics Unit, Massachusetts General Hospital, Charlestown, Massachusetts 02148 USA.
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↵Corresponding author.
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E-MAIL xcheng{at}emory.edu; FAX (404) 727-3746.
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- Received March 24, 1999.
- Accepted May 13, 1999.
- Cold Spring Harbor Laboratory Press
