Comparative molecular dynamics simulation of apo and holo forms of the P53 mutant C176F: a structural perspective
Zinc fingers represent a highly diverse structural domain, with P53 being a notable example among zinc-dependent transcription factors. The folding patterns of proteins in the cell are heavily influenced by the concentration of zinc. The potential for zinc loss arises due to its dysregulation and th...
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| Format: | Article |
| Language: | English |
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Taylor & Francis Group
2024-12-01
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| Series: | Journal of Taibah University for Science |
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| Online Access: | https://www.tandfonline.com/doi/10.1080/16583655.2023.2297457 |
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| author | R. Hephzibah Cathryn C. George Priya Doss |
| author_facet | R. Hephzibah Cathryn C. George Priya Doss |
| author_sort | R. Hephzibah Cathryn |
| collection | DOAJ |
| description | Zinc fingers represent a highly diverse structural domain, with P53 being a notable example among zinc-dependent transcription factors. The folding patterns of proteins in the cell are heavily influenced by the concentration of zinc. The potential for zinc loss arises due to its dysregulation and the frequent occurrence of tumorigenic P53 mutations. This could lead to significant consequences such as protein misfolding and a reduction in tumor-suppressing capabilities. To gain deeper insights into the structural conformation, stability, flexibility, and compactness of the zinc-binding mutation C176F, a comprehensive comparative computational analysis was conducted on the wildtype (WT) and mutant (MT) P53 in the presence (Holo) and absence (Apo) of zinc. This analysis was performed using molecular dynamic simulation. The overall observation was that the mutation in C176F reduces the metal binding affinity and results in less stability in the Apo and Holo P53 MT protein. |
| format | Article |
| id | doaj-art-cc34cc7f08a44a18a41dd2c24f7da223 |
| institution | Kabale University |
| issn | 1658-3655 |
| language | English |
| publishDate | 2024-12-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | Journal of Taibah University for Science |
| spelling | doaj-art-cc34cc7f08a44a18a41dd2c24f7da2232024-12-17T11:38:48ZengTaylor & Francis GroupJournal of Taibah University for Science1658-36552024-12-0118110.1080/16583655.2023.2297457Comparative molecular dynamics simulation of apo and holo forms of the P53 mutant C176F: a structural perspectiveR. Hephzibah Cathryn0C. George Priya Doss1Laboratory of Integrative Genomics, Department of Integrative Biology, School of BioSciences and Technology, Vellore Institute of Technology (VIT), Vellore, IndiaLaboratory of Integrative Genomics, Department of Integrative Biology, School of BioSciences and Technology, Vellore Institute of Technology (VIT), Vellore, IndiaZinc fingers represent a highly diverse structural domain, with P53 being a notable example among zinc-dependent transcription factors. The folding patterns of proteins in the cell are heavily influenced by the concentration of zinc. The potential for zinc loss arises due to its dysregulation and the frequent occurrence of tumorigenic P53 mutations. This could lead to significant consequences such as protein misfolding and a reduction in tumor-suppressing capabilities. To gain deeper insights into the structural conformation, stability, flexibility, and compactness of the zinc-binding mutation C176F, a comprehensive comparative computational analysis was conducted on the wildtype (WT) and mutant (MT) P53 in the presence (Holo) and absence (Apo) of zinc. This analysis was performed using molecular dynamic simulation. The overall observation was that the mutation in C176F reduces the metal binding affinity and results in less stability in the Apo and Holo P53 MT protein.https://www.tandfonline.com/doi/10.1080/16583655.2023.2297457P53tumour suppressorzinc binding residuesDNA-binding domainzinc fingermolecular dynamic simulation |
| spellingShingle | R. Hephzibah Cathryn C. George Priya Doss Comparative molecular dynamics simulation of apo and holo forms of the P53 mutant C176F: a structural perspective Journal of Taibah University for Science P53 tumour suppressor zinc binding residues DNA-binding domain zinc finger molecular dynamic simulation |
| title | Comparative molecular dynamics simulation of apo and holo forms of the P53 mutant C176F: a structural perspective |
| title_full | Comparative molecular dynamics simulation of apo and holo forms of the P53 mutant C176F: a structural perspective |
| title_fullStr | Comparative molecular dynamics simulation of apo and holo forms of the P53 mutant C176F: a structural perspective |
| title_full_unstemmed | Comparative molecular dynamics simulation of apo and holo forms of the P53 mutant C176F: a structural perspective |
| title_short | Comparative molecular dynamics simulation of apo and holo forms of the P53 mutant C176F: a structural perspective |
| title_sort | comparative molecular dynamics simulation of apo and holo forms of the p53 mutant c176f a structural perspective |
| topic | P53 tumour suppressor zinc binding residues DNA-binding domain zinc finger molecular dynamic simulation |
| url | https://www.tandfonline.com/doi/10.1080/16583655.2023.2297457 |
| work_keys_str_mv | AT rhephzibahcathryn comparativemoleculardynamicssimulationofapoandholoformsofthep53mutantc176fastructuralperspective AT cgeorgepriyadoss comparativemoleculardynamicssimulationofapoandholoformsofthep53mutantc176fastructuralperspective |