Full Article: PDF
Scientific Object Identifier: http://s-o-i.org/1.1/TAS-06-158-16
DOI: https://dx.doi.org/10.15863/TAS.2026.06.158.16
Language: English
Citation: Mengnorova, M.J. (2026). Molecular docking studies of indole-3-acetic acid and its zinc(II) complex with the TIR1 auxin receptor. ISJ Theoretical & Applied Science, 06 (158), 277-280. Soi: https://s-o-i.org/1.1/TAS-06-158-16 Doi: https://dx.doi.org/10.15863/TAS.2026.06.158.16 |
Pages: 277-280
Published: 30.06.2026
Abstract: Indole-3-acetic acid (IAA) is one of the most important natural auxins involved in plant growth regulation, cell elongation, differentiation, and developmental processes. The biological activity of auxins is mainly associated with their recognition by auxin receptor proteins, among which TIR1 (Transport Inhibitor Response 1) plays a key role in auxin-dependent signaling pathways. In the present study, molecular docking analysis was carried out to investigate the interaction of free indole-3-acetic acid and its zinc(II) coordination complex with the TIR1 receptor protein. The zinc(II) complex contains one Zn(II) ion coordinated by two IAA ligands in a monodentate mode and one monoethanolamine molecule acting as a chelating ligand. Blind docking was performed using the CB-Dock2 server to identify the most favorable binding cavities and ligand-binding poses. The docking results showed that free IAA interacts with the TIR1 receptor with a best docking score of -6.8 kcal/mol, whereas the Zn(II) complex demonstrated a significantly stronger binding affinity with a best docking score of -8.8 kcal/mol. The enhanced binding of the Zn(II) complex may be related to the presence of two IAA fragments, increased molecular size, additional donor groups, and a more preorganized coordination structure around the zinc center. These results indicate that coordination of IAA with Zn(II) may modify and enhance its interaction with the TIR1 auxin receptor.
Key words: Indole-3-acetic acid, IAA, auxin, TIR1 receptor, zinc complex, monoethanolamine, molecular docking, CB-Dock2, binding energy.
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