Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16.
Details
Serval ID
serval:BIB_3B25C6F57F00
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16.
Journal
Genes and Development
ISSN
0890-9369[print], 0890-9369[linking]
Publication state
Published
Issued date
07/1999
Volume
13
Number
13
Pages
1692-1703
Language
english
Notes
Publication types: Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S.
Publication Status: ppublish
Publication Status: ppublish
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.
Keywords
Amino Acid Sequence, Crystallization, Crystallography, X-Ray, DNA/metabolism, DNA-Binding Proteins/metabolism, Gene Expression Regulation, Viral, Herpes Simplex Virus Protein Vmw65/chemistry, Herpes Simplex Virus Protein Vmw65/genetics, Herpesviridae/chemistry, Host Cell Factor C1, Macromolecular Substances, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Octamer Transcription Factor-1, Protein Conformation, Recombinant Fusion Proteins/genetics, Regulatory Sequences, Nucleic Acid, Sequence Alignment, Sequence Homology, Amino Acid, Simplexvirus/chemistry, Simplexvirus/physiology, Transcription Factors/metabolism, Transcriptional Activation
Pubmed
Web of science
Open Access
Yes
Create date
24/01/2008 16:36
Last modification date
20/08/2019 14:31
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