16VP
CONSERVED CORE OF THE HERPES SIMPLEX VIRUS TRANSCRIPTIONAL REGULATORY PROTEIN VP16
Summary for 16VP
| Entry DOI | 10.2210/pdb16vp/pdb |
| Descriptor | PROTEIN (VP16, VMW65, ATIF), SULFATE ION (3 entities in total) |
| Functional Keywords | transcriptional regulatory protein |
| Biological source | Human herpesvirus 1 (Herpes simplex virus type 1) |
| Cellular location | Virion tegument : P06492 |
| Total number of polymer chains | 1 |
| Total formula weight | 41672.35 |
| Authors | Liu, Y.,Gong, W.,Huang, C.C.,Herr, W.,Cheng, X. (deposition date: 1999-02-11, release date: 1999-07-28, Last modification date: 2023-12-27) |
| Primary citation | Liu, Y.,Gong, W.,Huang, C.C.,Herr, W.,Cheng, X. Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16. Genes Dev., 13:1692-1703, 1999 Cited by 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. PubMed: 10398682PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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