Abstract
The structures of the catalytic subunit of protein kinase CK2 from Zea mays complexed with Mg2+ and with analogs of ATP or GTP were determined to 2.2 Å resolution. Unlike most other protein kinases, CK2 from various sources shows 'dual-cosubstrate specificity', that is, the ability to efficiently use either ATP or GTP as a cosubstrate. The structures of these complexes demonstrate that water molecules are critical to switch the active site of CK2 from an ATP- to a GTP-compatible state. An understanding of the structural basis of dual-cosubstrate specificity may help in the design of drugs that target CK2 or other kinases with this property.
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Niefind, K., Pütter, M., Guerra, B. et al. GTP plus water mimic ATP in the active site of protein kinase CK2. Nat Struct Mol Biol 6, 1100–1103 (1999). https://doi.org/10.1038/70033
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DOI: https://doi.org/10.1038/70033
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