TAT PROTEIN FROM HUMAN IMMUNODEFICIENCY VIRUS FORMS A METAL-LINKED DIMER
TAT PROTEIN FROM HUMAN IMMUNODEFICIENCY VIRUS FORMS A METAL-LINKED DIMER
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DOI：
10.1126/science.2832944
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发表时间：
1988-04-01
期刊：
影响因子：
56.9
通讯作者：
PABO, CO
中科院分区：
文献类型：
--
作者：
FRANKEL, AD;BREDT, DS;PABO, CO
Tat是来自HIV的反活化蛋白，它与金属离子形成金属连接的二聚体，将每个单体上富含半胱氨酸的区域连接起来。这种新颖的排列方式不同于在其他真核调节蛋白中观察到的“锌指”结构域。紫外吸收光谱显示，Tat在每个单体上结合了两个Zn2+或两个Cd2+离子，而Tat-金属配合物的电泳显示，该蛋白形成了金属连接的二聚体。部分蛋白水解和圆二色光谱表明，金属结合主要作用于富含半胱氨酸的区域，而对其他区域的折叠影响相对较小。这些结果提示了生物学研究的新方向和药物设计的新方法。
Tat, the transactivating protein from HIV, forms a metal-linked dimer with metal ions bridging cysteine-rich regions from each monomer. This novel arrangement is distinct from the "zinc finger" domain observed in other eukaryotic regulatory proteins. Ultraviolet absorption spectra show that Tat binds two Zn2+ or two Cd2+ ions per monomer, and electrophoresis of the Tat-metal complexes demonstrates that the protein forms metal-linked dimers. Partial proteolysis and circular dichroism spectra suggest that metal binding has its primary effects in the cysteine-rich region and relatively little effect on the folding of other regions. These results suggest new directions for biological studies and new approaches to drug design.