Crystal structure of DNA-PKcs reveals a large open-ring cradle comprised of HEAT repeats

Bancinyane L. Sibanda (), Dimitri Y. Chirgadze () and Tom L. Blundell
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Bancinyane L. Sibanda: University of Cambridge, Old Addenbrooke’s site, 80 Tennis Court Road, Cambridge CB2 1GA, UK
Dimitri Y. Chirgadze: University of Cambridge, Old Addenbrooke’s site, 80 Tennis Court Road, Cambridge CB2 1GA, UK
Tom L. Blundell: University of Cambridge, Old Addenbrooke’s site, 80 Tennis Court Road, Cambridge CB2 1GA, UK

Nature, 2010, vol. 463, issue 7277, 118-121

Abstract: Turning the HEAT on DNA-PKcs Several members of the phosphatidylinositol-3-OH kinase (PI(3)K) family are involved in the response to DNA double-strand breaks. One of these, DNA-dependent protein kinase (DNA-PK), is comprised of three subunits, with the kinase activity residing in the catalytic subunit, DNA-PKcs. In this study, Tom Blundell and colleagues have solved the structure of human DNA-PKcs, at a resolution sufficient to see the overall folds. The structure reveals that the many HEAT repeats bend the protein into a circular structure. The kinase domain, encoded in the C-terminal domain, sits on one side of the structure. While the overall architecture of the catalytic subunit allows speculation about regions where conformational changes may occur, confirmation of such interactions awaits higher resolution data.

Date: 2010
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DOI: 10.1038/nature08648

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