ProNAB: database for binding affinities of protein–nucleic acid complexes and their mutants
| العنوان: | ProNAB: database for binding affinities of protein–nucleic acid complexes and their mutants |
|---|---|
| المؤلفون: | M. Michael Gromiha, Ambuj Srivastava, A. Kulandaisamy, Kannan Harini |
| المصدر: | Nucleic Acids Research |
| بيانات النشر: | Oxford University Press (OUP), 2021. |
| سنة النشر: | 2021 |
| مصطلحات موضوعية: | Database, Macromolecular Substances, AcademicSubjects/SCI00010, Mutant, Protein Data Bank (RCSB PDB), Proteins, Translation (biology), Biology, PROSITE, computer.software_genre, DNA-Binding Proteins, Dissociation constant, Nucleic Acids, GenBank, Mutation, Genetics, Nucleic acid, Database Issue, UniProt, Databases, Protein, computer, Protein Binding |
| الوصف: | Protein–nucleic acid interactions are involved in various biological processes such as gene expression, replication, transcription, translation and packaging. The binding affinities of protein–DNA and protein–RNA complexes are important for elucidating the mechanism of protein–nucleic acid recognition. Although experimental data on binding affinity are reported abundantly in the literature, no well-curated database is currently available for protein–nucleic acid binding affinity. We have developed a database, ProNAB, which contains more than 20 000 experimental data for the binding affinities of protein–DNA and protein–RNA complexes. Each entry provides comprehensive information on sequence and structural features of a protein, nucleic acid and its complex, experimental conditions, thermodynamic parameters such as dissociation constant (Kd), binding free energy (ΔG) and change in binding free energy upon mutation (ΔΔG), and literature information. ProNAB is cross-linked with GenBank, UniProt, PDB, ProThermDB, PROSITE, DisProt and Pubmed. It provides a user-friendly web interface with options for search, display, sorting, visualization, download and upload the data. ProNAB is freely available at https://web.iitm.ac.in/bioinfo2/pronab/ and it has potential applications such as understanding the factors influencing the affinity, development of prediction tools, binding affinity change upon mutation and design complexes with the desired affinity. |
| تدمد: | 1362-4962 0305-1048 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8389898bc7b67bc839d148a9d57e313 https://doi.org/10.1093/nar/gkab848 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....d8389898bc7b67bc839d148a9d57e313 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 13624962 03051048 |
|---|