Tat protein from human immunodeficiency virus forms a metal-linked dimer |
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Authors: | A D Frankel D S Bredt C O Pabo |
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Institution: | Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205. |
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Abstract: | 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. |
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