Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16.
Détails
ID Serval
serval:BIB_3B25C6F57F00
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16.
Périodique
Genes and Development
ISSN
0890-9369[print], 0890-9369[linking]
Statut éditorial
Publié
Date de publication
07/1999
Volume
13
Numéro
13
Pages
1692-1703
Langue
anglais
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
Résumé
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.
Mots-clé
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
Oui
Création de la notice
24/01/2008 16:36
Dernière modification de la notice
20/08/2019 14:31
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