Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration
Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration
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DOI：
10.1038/2345
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发表时间：
1998-10-01
期刊：
影响因子：
--
通讯作者：
Clore, GM
中科院分区：
文献类型：
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作者：
Cai, M;Huang, Y;Clore, GM
人类自动整合障碍因子 BAF（一种 21,000 M 二聚体）的溶液结构已通过 NMR 解析，包括广泛使用提供先验长程结构信息的偶极耦合。 BAF是一种高度进化保守的DNA结合蛋白，负责抑制逆转录病毒DNA的自动整合，从而促进逆转录病毒DNA整合到宿主染色体中。 BAF主要是螺旋状的，每个亚基由五个螺旋组成。二聚体的形状是拉长的，并且二聚体界面主要包括疏水性接触，辅以单盐桥。尽管与任何其他已知蛋白质家族不存在任何序列相似性，但螺旋 3-5 的拓扑结构与许多 DNA 结合蛋白的拓扑相似，其中螺旋 4 和 5 构成螺旋-转角-螺旋基序。提出了一种 BAF 与 DNA 相互作用的模型，该模型与结构和诱变数据一致。
The solution structure of the human barrier-to-autointegration factor, BAF, a 21,000 M, dimer, has been solved by NMR, including extensive use of dipolar couplings which provide a priori long range structural information. BAF is a highly evolutionarily conserved DNA binding protein that is responsible for inhibiting autointegration of retroviral DNA, thereby promoting integration of retroviral DNA into the host chromosome. BAF is largely helical, and each subunit is composed of five helices. The dimer is elongated in shape and the dimer interface comprises principally hydrophobic contacts supplemented by a single salt bridge. Despite the absence of any sequence similarity to any other known protein family, the topology of helices 3-5 is similar to that of a number of DNA binding proteins, with helices 4 and 5 constituting a helix-turn-helix motif. A model for the interaction of BAF with DNA that is consistent with structural and mutagenesis data is proposed.