Structural Basis of Wee Kinases Functionality and Inactivation by Diverse Small Molecule Inhibitors
朱进一 Zhu Jinyi
1
,
Rebecca A Cuellar
2
,
Norbert Berndt
1
,
Hee Eun Lee
1
,
Sanne H Olesen
1
,
Mathew Martin
1
,
Jeffrey T. Jensen
3
,
Gunda I Georg
2
,
3
Division
of Reproductive and Developmental Science, Oregon National Primate Research Center, Beaverton, Oregon 97006, United States
|
Publication type: Journal Article
Publication date: 2017-09-14
scimago Q1
wos Q1
SJR: 1.801
CiteScore: 11.5
Impact factor: 6.8
ISSN: 00222623, 15204804
PubMed ID:
28792760
Drug Discovery
Molecular Medicine
Abstract
Members of the Wee family of kinases negatively regulate the cell cycle via phosphorylation of CDK1 and are considered potential drug targets. Herein, we investigated the structure–function relationship of human Wee1, Wee2, and Myt1 (PKMYT1). Purified recombinant full-length proteins and kinase domain constructs differed substantially in phosphorylation states and catalytic competency, suggesting complex mechanisms of activation. A series of crystal structures reveal unique features that distinguish Wee1 and Wee2 from Myt1 and establish the structural basis of differential inhibition by the widely used Wee1 inhibitor MK-1775. Kinome profiling and cellular studies demonstrate that, in addition to Wee1 and Wee2, MK-1775 is an equally potent inhibitor of the polo-like kinase PLK1. Several previously unrecognized inhibitors of Wee kinases were discovered and characterized. Combined, the data provide a comprehensive view on the catalytic and structural properties of Wee kinases and a framework for the rational...
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87
Total citations:
87
Citations from 2024:
25
(28%)
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GOST
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Zhu Jinyi 朱. et al. Structural Basis of Wee Kinases Functionality and Inactivation by Diverse Small Molecule Inhibitors // Journal of Medicinal Chemistry. 2017. Vol. 60. No. 18. pp. 7863-7875.
GOST all authors (up to 50)
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Zhu Jinyi 朱., Cuellar R. A., Berndt N., Lee H. E., Olesen S. H., Martin M., Jensen J. T., Georg G. I., Schönbrunn E. Structural Basis of Wee Kinases Functionality and Inactivation by Diverse Small Molecule Inhibitors // Journal of Medicinal Chemistry. 2017. Vol. 60. No. 18. pp. 7863-7875.
Cite this
RIS
Copy
TY - JOUR
DO - 10.1021/acs.jmedchem.7b00996
UR - https://doi.org/10.1021/acs.jmedchem.7b00996
TI - Structural Basis of Wee Kinases Functionality and Inactivation by Diverse Small Molecule Inhibitors
T2 - Journal of Medicinal Chemistry
AU - Zhu Jinyi, 朱进一
AU - Cuellar, Rebecca A
AU - Berndt, Norbert
AU - Lee, Hee Eun
AU - Olesen, Sanne H
AU - Martin, Mathew
AU - Jensen, Jeffrey T.
AU - Georg, Gunda I
AU - Schönbrunn, Ernst
PY - 2017
DA - 2017/09/14
PB - American Chemical Society (ACS)
SP - 7863-7875
IS - 18
VL - 60
PMID - 28792760
SN - 0022-2623
SN - 1520-4804
ER -
Cite this
BibTex (up to 50 authors)
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@article{2017_Zhu Jinyi,
author = {朱进一 Zhu Jinyi and Rebecca A Cuellar and Norbert Berndt and Hee Eun Lee and Sanne H Olesen and Mathew Martin and Jeffrey T. Jensen and Gunda I Georg and Ernst Schönbrunn},
title = {Structural Basis of Wee Kinases Functionality and Inactivation by Diverse Small Molecule Inhibitors},
journal = {Journal of Medicinal Chemistry},
year = {2017},
volume = {60},
publisher = {American Chemical Society (ACS)},
month = {sep},
url = {https://doi.org/10.1021/acs.jmedchem.7b00996},
number = {18},
pages = {7863--7875},
doi = {10.1021/acs.jmedchem.7b00996}
}
Cite this
MLA
Copy
Zhu Jinyi, 朱进一, et al. “Structural Basis of Wee Kinases Functionality and Inactivation by Diverse Small Molecule Inhibitors.” Journal of Medicinal Chemistry, vol. 60, no. 18, Sep. 2017, pp. 7863-7875. https://doi.org/10.1021/acs.jmedchem.7b00996.