Tat Protein from Human Immunodeficiency Virus Forms a Metal-Linked Dimer

作者：Alan D. Frankel, David S. Bredt, Carl O. Pabo · 发表于：Science · 年份：1988 · DOI：10.1126/science.2832944 · 被引用次数：458 · 研究领域：RNA and protein synthesis mechanisms、Trace Elements in Health、HIV Research and Treatment

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.