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

Frankel, Alan D., Bredt, David S., Pabo, Carl O.·1988·Science

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 Zn 2+ or two Cd 2+ 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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Metadata

Authors
Frankel, A. D., Bredt, D. S., & Pabo, C. O.
Venue
Science
Published
1988-04
Volume
240
Issue
4848
Pages
70-73
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2006244184
Cited by
457
References
0
FWCI
15.99
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Tat Protein from Human Immunodeficiency Virus Forms a Metal-Linked Dimer. https://app.cochat.ai/papers/10.1126/science.2832944
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Frankel, A. D., Bredt, D. S., & Pabo, C. O. (1988). Tat Protein from Human Immunodeficiency Virus Forms a Metal-Linked Dimer. Science. https://doi.org/10.1126/science.2832944

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