دورية أكاديمية
Molecular docking of substituted pteridinones and pyrimidines to the ATP-binding site of the N-terminal domain of RSK2 and associated MM/GBSA and molecular field datasets.
| العنوان: | Molecular docking of substituted pteridinones and pyrimidines to the ATP-binding site of the N-terminal domain of RSK2 and associated MM/GBSA and molecular field datasets. |
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| المؤلفون: | Casalvieri KA; 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., Matheson CJ; 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., Backos DS; 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., Reigan P; 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. |
| المصدر: | Data in brief [Data Brief] 2020 Feb 28; Vol. 29, pp. 105347. Date of Electronic Publication: 2020 Feb 28 (Print Publication: 2020). |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier B.V Country of Publication: Netherlands NLM ID: 101654995 Publication Model: eCollection Cited Medium: Internet ISSN: 2352-3409 (Electronic) Linking ISSN: 23523409 NLM ISO Abbreviation: Data Brief Subsets: PubMed not MEDLINE |
| أسماء مطبوعة: | Original Publication: [Amsterdam] : Elsevier B.V., [2014]- |
| مستخلص: | 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). (© 2020 The Author(s).) |
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| فهرسة مساهمة: | Keywords: Inhibitor; Kinase; Molecular docking; QSAR; RSK2; Structure-activity relationship |
| تواريخ الأحداث: | Date Created: 20200327 Latest Revision: 20200928 |
| رمز التحديث: | 20231215 |
| مُعرف محوري في PubMed: | PMC7082523 |
| DOI: | 10.1016/j.dib.2020.105347 |
| PMID: | 32211459 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 2352-3409 |
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| DOI: | 10.1016/j.dib.2020.105347 |