Liu Y, Gong W, Huang C C, Herr W, Cheng X
Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724, USA.
Genes Dev. 1999 Jul 1;13(13):1692-703. doi: 10.1101/gad.13.13.1692.
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.
感染时，单纯疱疹病毒（HSV）病毒体蛋白VP16（Vmw65；αTIF）在HSV立即早期启动子中称为TAATGARAT的VP16反应性顺式调节元件上，与两种细胞蛋白HCF和Oct-1形成转录调节复合物——VP16诱导复合物。不同HSV VP16序列的比较揭示了一个保守的核心区域，该区域足以形成VP16诱导复合物。VP16核心的晶体结构已在2.1埃分辨率下确定。结果揭示了一种新颖的、座椅状的蛋白质结构。结合突变型VP16蛋白的活性，游离VP16的结构表明它包含（1）一个无序的羧基末端区域，该区域在VP16诱导复合物中与HCF、Oct-1和DNA结合，以及（2）一个参与病毒体组装并具有区分TAATGARAT VP16反应元件的新型DNA结合表面的结构化区域。
