RECONSTRUCTION OF A MODEL OF A MULTIPROTEIN COMPLEX CRITICAL FOR ATG8 LIPIDATION DURING AUTOPHAGOSOME FORMATION IN PLANTS
DOI:
https://doi.org/10.15407/dopovidi2025.01.068Keywords:
autophagy, Arabidopsis thaliana, ATG proteins, molecular dynamicsAbstract
Autophagy represents a fundamental cellular process, whereby molecules and subcellular elements, including nucleic acids, proteins, lipids, and organelles, are eliminated through lysosome-mediated degradation. This process plays a crucial role in maintaining cellular homeostasis, promotes differentiation, supports development and contributes to cell survival.
The research is devoted to the study of the molecular nature of the interaction of proteins of the ATG12- ATG5-ATG16 and ATG8 orthologs of plant and human conjugation systems with subsequent in silico docking for the implementation of future integration into a multimeric complex with the addition of phosphoinositide interacting protein 2 (WIPI2), and their subsequent reproduction with animal orthologs of autophagosome biogenesis mating systems.
A thorough comprehension of both theoretical and practical aspects of modern computing is essential for the development of robust computational methods. The introduction of these methods combined with an in-depth review of the scientific literature provides a solid foundation for the study of protein conformational changes. By creating calculated variations of a known protein structure and providing the appropriate content for reproduction and interpretation of conformational changes, it is possible to identify functional states that align with the specific requirements of a given system. The employment of computer modeling methodologies permits the construction of structural models and the replication of intermolecular interactions. This enables an enhanced evaluation of the prospective interaction between future inhibitors or ligands and the target. The authors utilized in silico modeling to predict and elucidate potential interactions between the components of a multi-protein complex.
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