Structural correlates for enhanced stability in the E2 DNA-binding domain from bovine papillomavirus.
Structural correlates for enhanced stability in the E2 DNA-binding domain from bovine papillomavirus.
复制标题
牛乳头瘤病毒 E2 DNA 结合域稳定性增强的结构相关性。
DOI：
10.1021/bi991633x
复制
发表时间：
1999
期刊：
影响因子：
2.9
通讯作者：
Baleja,JD
中科院分区：
文献类型：
--
作者：
Veeraraghavan,S;Mello,CC;Androphy,EJ;Baleja,JD
乳头瘤病毒E2蛋白参与病毒DNA复制和转录调控。我们已经解决了从牛乳头瘤病毒（BPV-1）的E2蛋白的DNA结合结构域的溶液结构。结构计算使用2222距离和158二面角约束的同源二聚体（共202个残基），这是来自同源和异源多维核磁共振（NMR）光谱数据。当叠加到平均值时，单体结构化区域的均方根偏差对于主链原子为0.73 ± 0.10 μ m，对于重原子为1.42 ± 0.16 μ m。本研究中使用的101个残基构建体（残基310 - 410）比包含C末端85个氨基酸残基的最小结构域（残基326 - 410）稳定约4.5 kcal/mol。BPV-1 E2的核心结构域与其他乳头瘤病毒E2蛋白的相应区域相似。然而，在这里，额外的N-末端16个残基形成覆盖二聚体界面处的空腔的瓣，并在DNA结合中发挥作用。N-末端延伸和核心结构域中的残基之间的相互作用与较长形式的蛋白质相对于最小结构域的更大稳定性相关。
Papillomaviral E2 proteins participate in viral DNA replication and transcriptional regulation. We have solved the solution structure of the DNA-binding domain of the E2 protein from bovine papillomavirus (BPV-1). The structure calculation used 2222 distance and 158 dihedral angle restraints for the homodimer (202 residues in total), which were derived from homonuclear and heteronuclear multidimensional nuclear magnetic resonance (NMR) spectroscopic data. The root-mean-square deviation for structured regions of the monomer when superimposed to the average is 0.73 ± 0.10 Å for backbone atoms and 1.42 ± 0.16 Å for heavy atoms. The 101 residue construct used in this study (residues 310−410) is about 4.5 kcal/mol more stable than a minimal domain comprising the C-terminal 85 amino acid residues (residues 326−410). The structure of the core domain contained within BPV-1 E2 is similar to the corresponding regions of other papillomaviral E2 proteins. Here, however, the extra N-terminal 16 residues form a flap that covers a cavity at the dimer interface and play a role in DNA binding. Interactions between residues in the N-terminal extension and the core domain correlate with the greater stability of the longer form of the protein relative to the minimal domain.