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Updated: Aug 17, 2026

Identification of Kinase-substrate Pairs Using High Throughput Screening
Published on: August 29, 2015
GTP plus water mimic ATP in the active site of protein kinase CK2
K Niefind1, M Pütter, B Guerra
1Universität zu Köln, Institut für Biochemie, Zülpicher Strabetae 47, D-50674 Köln, Germany. Karsten.Niefind@uni-koeln.de
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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