Molecular Determinant s Elucidate the Selectivity in Abscisic acid Receptor and HAB1 Protein Interactions
| Autor: | Jing-Fang Yang, Chun-Yan Yin, Di Wang, Chen-Yang Jia, Ge-Fei Hao, Guang-Fu Yang |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Phosphatase
Sequence alignment 02 engineering and technology 010402 general chemistry 01 natural sciences Protein–protein interaction abscisic acid lcsh:Chemistry chemistry.chemical_compound Receptor Abscisic acid PYR/PYL/RCARs Original Research Pyrabactin Pyr1 selectivity General Chemistry 021001 nanoscience & nanotechnology Ligand (biochemistry) pyrabactin molecular dynamics 0104 chemical sciences Chemistry chemistry lcsh:QD1-999 Biophysics 0210 nano-technology |
| Zdroj: | Frontiers in Chemistry, Vol 8 (2020) Frontiers in Chemistry |
| DOI: | 10.21203/rs.2.22596/v1 |
| Popis: | The abscisic acid (ABA), as a pivotal plant hormone, plays a key role in controlling the life cycle and adapting to the environmental stresses. The receptors of ABA are the Pyrabactin Resistance /Pyrabactin Resistance -Like/Regulatory Component of ABA Receptors (PYR/PYL/RCAR, PYLs for simplicity), which regulate the Protein Phosphatase 2Cs (PP2Cs) in the signal pathway. As an important ABA mimicking ligand, Pyrabactin shows the activation function to parts of members of PYLs, such as PYR1 and PYL1. Due to the antagonism of Pyrabactin to PYL2, it was used as a probe to discover a part of ABA receptors. Since then, many researchers have been trying to find out the determinants of the selective regulation of PYLs and PP2Cs interaction. However, the roles of residues on the selective regulation of PYR1/PYL2 and PP2Cs interaction induced by Pyrabactin are still ambiguous. This research investigated the selective activation mechanism of Pyrabactin through the sequence alignment, molecular docking, molecular dynamics simulation, and binding free energy calculation. Furthermore, the electrostatic and hydrophobic interaction differences induced by Pyrabactin and agonists were compared. The results indicate that Leu137/Val114, Ser85/Ser89, and Gly86/Gly90 from the pocket and gate of PYR1/PYL2 are the vital residues for the selective activation of Pyrabactin. Meanwhile, the electrostatic interaction between PP2Cs and PYLs complexed with agonists was improved. This mechanism provides strong support for the design of selective agonists and antagonists. |
| Databáze: | OpenAIRE |
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