GTP plus water mimic ATP in the active site of protein kinase CK2 |
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Authors: | Niefind K Pütter M Guerra B Issinger O G Schomburg D |
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Affiliation: | Universit?t zu K?ln, Institut für Biochemie, Zülpicher Strabetae 47, D-50674 K?ln, Germany. Karsten.Niefind@uni-koeln.de |
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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 A 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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