The Cambridge Crystallographic Data Centre (CCDC), 12 Union Road, Cambridge, CB2 1EZ, U.K.
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, U.K.
J Chem Inf Model. 2020 Apr 27;60(4):1911-1916. doi: 10.1021/acs.jcim.9b00996. Epub 2020 Apr 2.
Methods that survey protein surfaces for binding hotspots can help to evaluate target tractability and guide exploration of potential ligand binding regions. Fragment Hotspot Maps builds upon interaction data mined from the CSD (Cambridge Structural Database) and exploits the idea of identifying hotspots using small chemical fragments, which is now widely used to design new drug leads. Prior to this publication, Fragment Hotspot Maps was only publicly available through a web application. To increase the accessibility of this algorithm we present the Hotspots API (application programming interface), a toolkit that offers programmatic access to the core Fragment Hotspot Maps algorithm, thereby facilitating the interpretation and application of the analysis. To demonstrate the package's utility, we present a workflow which automatically derives protein hydrogen-bond constraints for molecular docking with GOLD. The Hotspots API is available from https://github.com/prcurran/hotspots under the MIT license and is dependent upon the commercial CSD Python API.
方法调查蛋白质表面的结合热点，可以帮助评估目标的可及性，并指导探索潜在的配体结合区域。片段热点图基于从 CSD（剑桥结构数据库）挖掘的交互数据，并利用使用小化学片段识别热点的想法，现在广泛用于设计新的药物先导物。在本出版物之前，片段热点图仅通过网络应用程序公开提供。为了提高此算法的可访问性，我们提供了 Hotspots API（应用程序编程接口），这是一个工具包，提供了对核心片段热点图算法的编程访问，从而促进了分析的解释和应用。为了演示该软件包的实用性，我们展示了一个自动为分子对接生成蛋白质氢键约束的工作流程，使用 GOLD。Hotspots API 可从 https://github.com/prcurran/hotspots 获得，遵循 MIT 许可证，并且依赖于商业 CSD Python API。
