| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1365199 | Bioorganic & Medicinal Chemistry Letters | 2008 | 5 Pages |
Abstract
Non-ATP competitive pyrimidine-based inhibitors of CaMKIIδ were identified. Computational studies were enlisted to predict the probable mode of binding. The results of the computational studies led to the design of ATP competitive inhibitors with optimized hinge interactions. Inhibitors of this class possessed improved enzyme and cellular activity compared to early leads.
Graphical abstractPyrimidine-based inhibitors of CaMKIIδ were identified. Through computational studies, a probable binding mode was identified leading to the design of ATP competitive inhibitors with improved potency, potential hinge interactions, and potent cellular activity.Figure optionsDownload full-size imageDownload as PowerPoint slide
Related Topics
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Authors
Babu Mavunkel, Yong-jin Xu, Bindu Goyal, Don Lim, Qing Lu, Zheng Chen, Dan-Xiong Wang, Jeffrey Higaki, Indrani Chakraborty, Albert Liclican, Steve Sideris, Maureen Laney, Ulrike Delling, Rosanne Catalano, Linda S. Higgins, Hui Wang, Jing Wang, Ying Feng,