Structural basis of lentiviral subversion of a cellular protein degradation pathway

David Schwefel, Harriet C. T. Groom, Virginie C. Boucherit, Evangelos Christodoulou, Philip A. Walker, Jonathan P. Stoye, Kate N. Bishop and Ian A. Taylor ()
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David Schwefel: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Harriet C. T. Groom: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Virginie C. Boucherit: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Evangelos Christodoulou: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Philip A. Walker: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Jonathan P. Stoye: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Kate N. Bishop: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Ian A. Taylor: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK

Nature, 2014, vol. 505, issue 7482, 234-238

Abstract: The crystal structure of a ternary complex of the lentiviral accessory protein Vpx with the E3 ligase substrate adaptor DCAF1 and the HIV-1 restriction factor SAMHD1 shows how Vpx recruits SAMHD1 to the cell’s ubiquitination machinery.

Date: 2014
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DOI: 10.1038/nature12815

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