Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16
AUTOR(ES)
Liu, Yu
FONTE
Cold Spring Harbor Laboratory Press
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=316849Documentos Relacionados
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