Casalvieri Kimberly A, Matheson Christopher J, Backos Donald S, Reigan Philip
Department of Pharmaceutical Sciences, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of Colorado Anschutz Medical Campus, 12850 East Montview Boulevard, Aurora, CO, 80045, USA.
Data Brief. 2020 Feb 28;29:105347. doi: 10.1016/j.dib.2020.105347. eCollection 2020 Apr.
The data have been obtained for a series of substituted pteridinones and pyrimidines that were developed based on BI-D1870 to establish a structure-activity relationship for RSK inhibition. The 19 compounds, 12 of these with R- and S-isomeric forms, were docked into the ATP-binding site of the N-terminal domain of the RSK2 kinase using Schrodinger Glide. The binding conformations of these molecules and their interactions with RSK2 may inform the development of further small molecule RSK inhibitors. The molecular mechanics energies combined with the generalized Born and surface area continuum solvation (MM-BGSA) method was used to estimate the free energy of binding of the small molecules with RSK2. The molecular field characteristics of the docked confirmations of the inhibitors was examined using Cresset Forge software. The synthesis and evaluation of these compounds was reported in the related research article: Substituted pteridinones as p90 ribosomal S6 protein kinase 2 (RSK2) inhibitors: a structure-activity study (Casalvieri et al., 2020).
已获得一系列基于BI-D1870开发的取代蝶啶酮和嘧啶的数据，以建立RSK抑制的构效关系。这19种化合物中有12种具有R-和S-异构体形式，使用Schrodinger Glide将它们对接至RSK2激酶N端结构域的ATP结合位点。这些分子的结合构象及其与RSK2的相互作用可能为进一步开发小分子RSK抑制剂提供信息。采用分子力学能量结合广义玻恩和表面积连续溶剂化（MM-BGSA）方法估算小分子与RSK2的结合自由能。使用Cresset Forge软件检查抑制剂对接确认的分子场特征。这些化合物的合成和评价在相关研究文章《取代蝶啶酮作为p90核糖体S6蛋白激酶2（RSK2）抑制剂：构效关系研究》（Casalvieri等人，2020年）中有报道。
