Performance of 3D-database molecular docking studies into homology models
| Autor: | John Eksterowicz, Peter D. J. Grootenhuis, C. Oshiro, J.K. Lanctot, Erik Evensen, Michelle Lamb, Robert V. Stanton, Erin K. Bradley, Santosh Putta |
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| Přispěvatelé: | Molecular and Computational Toxicology |
| Jazyk: | angličtina |
| Rok vydání: | 2004 |
| Předmět: |
Models
Molecular Binding Sites biology Molecular model Databases Factual Stereochemistry Chemistry Cyclin-Dependent Kinase 2 Active site Coagulation factor VIIa Quantitative Structure-Activity Relationship Factor VIIa Factor VII Crystallography X-Ray Sequence identity Docking (molecular) Drug Discovery biology.protein CDC2-CDC28 Kinases Molecular Medicine Combinatorial Chemistry Techniques Homology modeling Binding site Protein Binding |
| Zdroj: | Oshiro, C, Bradley, E K, Eksterowicz, J E, Evensen, E, Lamb, M L, Lanctot, J K, Putta, S, Stanton, R V & Grootenhuis, P D J 2004, ' Performance of 3D-database molecular docking studies into homology models ', Journal of Medicinal Chemistry, vol. 47, no. 3, pp. 764-7 . https://doi.org/10.1021/jm0300781 Journal of Medicinal Chemistry, 47(3), 764-7. American Chemical Society |
| ISSN: | 1520-4804 0022-2623 |
| DOI: | 10.1021/jm0300781 |
| Popis: | The performance of docking studies into protein active sites constructed by homology model building was investigated using CDK2 and factor VIIa screening data sets. When the sequence identity between model and template near the binding site area is greater than approximately 50%, roughly 5 times more active compounds are identified than would be found randomly. This performance is comparable to docking to crystal structures. |
| Databáze: | OpenAIRE |
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