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Molecular Mechanism of Brassinosteroid Perception by the Plant Growth Receptor BRI1
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Abstract
Brassinosteroids (BRs) are essential phytohormones, which bind to the plant receptor, BRI1, to regulate various physiological processes. The molecular mechanism of the perception of BRs by the ectodomain of BRI1 remains not fully understood. It also remains elusive why a substantial difference in biological activity exists between the BRs. In this work, we study the binding mechanisms of the two most bioactive BRs, brassinolide (BLD) and castasterone (CAT), using molecular dynamics simulations. We report free-energy landscapes of the binding processes of both ligands, as well as detailed ligand binding pathways. Our results suggest that CAT has a lower binding affinity compared to BLD due to its inability to form hydrogen-bonding interactions with a tyrosine residue in the island domain of BRI1. We uncover a conserved nonproductive binding state for both BLD and CAT, which is more stable for CAT and may further contribute to the bioactivity difference. Finally, we validate past observations about the conformational restructuring and ordering of the island domain upon BLD binding. Overall, this study provides new insights into the fundamental mechanism of the perception of the two most bioactive BRs, which may create new avenues for genetic and agrochemical control of their signaling cascade.
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Metadata
- Authors
- Aldukhi, F., Deb, A., Zhao, C., Moffett, A. S., & Shukla, D.
- Affiliations
- University of Illinois Urbana-Champaign (US)
- Jadavpur University (IN)
- National Center for Supercomputing Applications (US)
- Corresponding author
- Shukla, Diwakar
- Venue
- The Journal of Physical Chemistry B
- Publisher
- American Chemical Society (ACS)
- Published
- 2019-12-24
- Volume
- 124
- Issue
- 2
- Pages
- 355-365
- ISSN
- 1520-5207 (ISSN-L)
- 1520-6106
- OpenAlex
- W2997612699
- Cited by
- 29
- References
- 70
- Citations by year
- 2026: 2 · 2025: 6 · 2024: 6 · 2023: 2 · 2022: 7 · 2021: 5 · 2020: 1
- FWCI
- 2.40
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- Locations
- The Journal of Physical Chemistry B (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- Foundation for Food and Agriculture Research
- Department of Biotechnology , Ministry of Science and Technology
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- brassinosteroids, brassinolide, castasterone, ligand binding mechanism, receptor tyrosine kinase, hydrogen bonding, free energy landscape, conformational change, plant hormone signaling
- MeSH terms
- Cholestanols, Hydrogen Bonding, Ligands, Models, Chemical, Protein Binding, Protein Conformation, Protein Kinases, Steroids, Heterocyclic, Thermodynamics, Tyrosine, Arabidopsis, Arabidopsis Proteins, Molecular Dynamics Simulation, Brassinosteroids
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