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16VP

CONSERVED CORE OF THE HERPES SIMPLEX VIRUS TRANSCRIPTIONAL REGULATORY PROTEIN VP16

Summary for 16VP
Entry DOI10.2210/pdb16vp/pdb
DescriptorPROTEIN (VP16, VMW65, ATIF), SULFATE ION (3 entities in total)
Functional Keywordstranscriptional regulatory protein
Biological sourceHuman herpesvirus 1 (Herpes simplex virus type 1)
Cellular locationVirion tegument : P06492
Total number of polymer chains1
Total formula weight41672.35
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 citationLiu, 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: 10398682
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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