@article{335cfe40ba9811dc9626000ea68e967b,
title = "GTP plus water mimics ATP in the active site of protein kianse CK2",
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.",
author = "K Niefind and M P{\"u}tter and B Guerra and Issinger, \{O G\} and D Schomburg",
year = "1999",
doi = "10.1038/70033",
language = "English",
volume = "6",
pages = "1100--1110",
journal = "Nature Structural Biology",
issn = "1072-8368",
publisher = "Nature Research",
number = "12",
}