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The DNA-binding domain of HIV-1 integrase has an SH3-like fold

Nature Structural Biology volume 2, pages 807–810 (1995)Cite this article

Abstract

We have determined the solution structure of the DNA-binding domain of HIV-1 integrase by nuclear magnetic resonance spectroscopy. In solution, this carboxy-terminal region of integrase forms a homodimer, consisting of two structures that closely resemble Src-homology 3 (SH3) domains. Lys 264, previously identified by mutagenesis studies to be important for DNA binding of the integrase, as well as several adjacent basic amino acids are solvent exposed. The identification of an SH3-like domain in integrase provides a new potential target for drug design.

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Author information

Authors and Affiliations

  1. Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands

    Astrid P.A.M. Eijkelenboom, Rolf Boelens, Robert Kaptein & Karl Hård

  2. Division of Molecular Biology, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX, Amsterdam, The Netherlands

    Ramon A. Puras Lutzke & Ronald H.A. Plasterk

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  1. Astrid P.A.M. Eijkelenboom
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Eijkelenboom, A., Puras Lutzke, R., Boelens, R. et al. The DNA-binding domain of HIV-1 integrase has an SH3-like fold. Nat Struct Mol Biol 2, 807–810 (1995). https://doi.org/10.1038/nsb0995-807

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