ZINC-FINGER PROTEINS
ZINC-FINGER PROTEINS
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DOI：
10.1016/0959-440x(93)90195-q
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发表时间：
1993-02-01
影响因子：
6.8
通讯作者：
BERG, JM
中科院分区：
文献类型：
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作者：
BERG, JM
在过去的一年里，关于各类锌指蛋白的结构及其识别特定核酸靶标的机制已经取得了相当大的进展。 NMR 和 X 射线结构均已可用于酵母蛋白 GAL4 的 DNA 结合结构域。这些揭示了 Zn2(Cys)6 双核簇的详细结构以及结合 DNA 的伴随结构。间接研究已经建立了 TFIIIA-5S RNA 基因复合体结构的模型。此外，关于不变金属结合和疏水残基在稳定锌指结构中的作用，已经有了更详细的数据。有关 TFIIIA 类锌指的结构信息指导了实验，这些实验导致了与 DNA 结合位点偏好相关的潜在有用规则。锌在逆转录病毒核衣壳蛋白生物学功能中的作用也变得更加清晰。
Considerable progress has been made over the past year concerning the structures of various classes of zinc-finger proteins and the mechanisms by which they recognize particular nucleic acid targets. Both NMR and X-ray structures have become available for the DNA-binding domain of the yeast protein GAL4. These have revealed the detailed architecture of the Zn2(Cys)6 binuclear cluster and the accompanying structure that binds DNA. Indirect studies have yielded models for the structure of the TFIIIA-5S RNA gene complex. In addition, more detailed data has become available concerning the roles of the invariant metal-binding and hydrophobic residues in stabilizing the zinc-finger structure. Structural information concerning the TFIIIA-like zinc fingers has guided experiments that are leading to potentially useful rules relating to DNA binding site preference. The role of zinc in the biological function of retroviral nucleocapsid proteins has also become clearer.