Kinase Atlas: Druggability Analysis of Potential Allosteric Sites in Kinases
| Autor: | Sandor Vajda, Justin Rettenmaier, Adrian Whitty, David Hall, György M. Keserü, Dima Kozakov, Krister J. Barkovich, James A. Wells, Christine Yueh, Andrey Alekseenko, Bing Xia, Kathryn A. Porter |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Models
Molecular Protein Conformation Allosteric regulation Druggability Computational biology 01 natural sciences Article 03 medical and health sciences Drug Development Drug Discovery Animals Humans Binding site Databases Protein Protein Kinase Inhibitors 030304 developmental biology 0303 health sciences Chemistry Kinase Extramural computer.file_format Protein Data Bank 0104 chemical sciences 010404 medicinal & biomolecular chemistry Molecular Medicine Protein Kinases computer Allosteric Site |
| Zdroj: | Journal of Medicinal Chemistry. 62:6512-6524 |
| ISSN: | 1520-4804 0022-2623 |
| DOI: | 10.1021/acs.jmedchem.9b00089 |
| Popis: | The inhibition of kinases has been pursued by the pharmaceutical industry for over 20 years. While the locations of the sites that bind type II and III inhibitors at or near the adenosine 5'-triphosphate binding sites are well defined, the literature describes 10 different regions that were reported as regulatory hot spots in some kinases and thus are potential target sites for type IV inhibitors. Kinase Atlas is a systematic collection of binding hot spots located at the above ten sites in 4910 structures of 376 distinct kinases available in the Protein Data Bank. The hot spots are identified by FTMap, a computational analogue of experimental fragment screening. Users of Kinase Atlas ( https://kinase-atlas.bu.edu ) may view summarized results for all structures of a particular kinase, such as which binding sites are present and how druggable they are, or they may view hot spot information for a particular kinase structure of interest. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|