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Autor Principal:	Quazi, Uzaif
Formato:	Recurso digital
Idioma:	inglés
Publicado:	Zenodo 2025
Subjects:	p53-SOG1 hybrid protein Hybrid transcription factor Synthetic transcription factors Cross-species DNA damage response Cancer therapy using hybrid proteins Tumor suppressor hybridization Computational protein design Molecular docking of transcription factors Molecular dynamics simulation of p53 DNA-binding efficiency in hybrid proteins Tetramerization of p53 hybrid Hybrid protein structural validation Synthetic biology and cancer therapeutics Bioinformatics in cancer drug development Protein engineering for tumor suppression In silico validation of transcription factors Functional validation of hybrid proteins Novel synthetic transcription factors Enhanced DNA-binding in hybrid p53 GROMACS simulation of DNA-binding proteins Computational approach to cancer treatment Protein hybridization for therapeutic applications p53 tumor suppressor engineering Molecular docking analysis of p53 hybrid Computational biology in cancer research Hybrid transcription factors in synthetic biology Structural modeling of DNA-binding proteins p53 and SOG1 fusion protein Protein stability analysis in hybrid molecules
Acceso en liña:	https://doi.org/10.5281/zenodo.14956162
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Table of Contents:

Understanding cross-species DNA damage response (DDR) regulators is critical  for advancing synthetic biology and cancer therapeutics. The tumor suppressor p53  (mammalian) and SOG1 (plant-specific) share functional parallels in regulating  DDR, yet their hybridization remains unexplored. This study presents a novel  hypothesis: a p53-SOG1 hybrid protein can retain p53’s tumor suppressive  function while incorporating SOG1’s regulatory efficiency, potentially offering  new avenues for cancer therapy.  To test this hypothesis, we designed and computationally validated the hybrid  protein using molecular docking, molecular dynamics (MD) simulations, and  structural validation. Docking studies revealed enhanced DNA-binding affinity  (ZDOCK score: 1453), stable structural dynamics (RMSD: 0.11 nm), and high  hydration stability (SASA: 373 nm²). Hydrogen bonding (1200+ H-bonds)  stabilized DNA binding. MolProbity analysis positioned the hybrid in the 100th  percentile for structural accuracy. Notably, the hybrid retains p53’s tetramerization  via the oligomerization (OD) and C-terminal (CTD) domains.  Our findings provide strong in silico support for the feasibility of a p53-SOG1  hybrid as a functional transcription factor. Future experimental directions include  expression in mammalian cells (HEK293T, HCT116), transcriptional activity  assays (qPCR, luciferase reporter), and DNA-binding kinetics via Surface Plasmon  Resonance (SPR). These steps will determine its viability for cancer therapeutics  and cross-species synthetic biology applications.

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