Tat protein from human immunodeficiency virus forms a metal-linked dimer - PubMed (original) (raw)

Comparative Study

. 1988 Apr 1;240(4848):70-3.

doi: 10.1126/science.2832944.

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Comparative Study

Tat protein from human immunodeficiency virus forms a metal-linked dimer

A D Frankel et al. Science. 1988.

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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