Download MendeleyGTP plus water mimic ATP in the active site of protein kinase CK2.
Niefind, K., Putter, M., Guerra, B., Issinger, O.G., Schomburg, D.(1999) Nat Struct Biol 6: 1100-1103
- PubMed: 10581548
- DOI: https://doi.org/10.1038/70033
- Primary Citation of Related Structures:
1DAW, 1DAY - PubMed 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.
Organizational Affiliation:
Universität zu Köln, Institut für Biochemie, Zülpicher Strabetae 47, D-50674 Köln, Germany. [email protected]
