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Lookup NU author(s): Joao Victor de De Souza Cunha, Dr Matthew Kondal, Dr Piotr Zaborniak, Dr Agnieszka Bronowska
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
© 2021 by the authors. Licensee MDPI, Basel, Switzerland.Phytosulfokine (PSK) is a phytohormone responsible for cell-to-cell communication in plants, playing a pivotal role in plant development and growth. The binding of PSK to its cognate receptor, PSKR1, is modulated by the formation of a binding site located between a leucine-rich repeat (LRR) domain of PSKR1 and the loop located in the receptor’s island domain (ID). The atomic resolution structure of the extracellular PSKR1 bound to PSK has been reported, however, the intrinsic dynamics of PSK binding and the architecture of the PSKR1 binding site remain to be under-stood. In this work, we used atomistic molecular dynamics (MD) simulations and free energy calculations to elucidate how the PSKR1 island domain (ID) loop forms and binds PSK. Moreover, we report a novel “druggable” binding site which could be exploited for the targeted modulation of the PSKR1-PSK binding by small molecules. We expect that our results will open new ways to modulate the PSK signalling cascade via small molecules, which can result in new crop control and agricul-tural applications.
Author(s): de Souza JV, Kondal M, Zaborniak P, Cairns R, Bronowska AK
Publication type: Article
Publication status: Published
Journal: International Journal of Molecular Sciences
Year: 2021
Volume: 22
Issue: 4
Pages: 1-14
Online publication date: 11/02/2021
Acceptance date: 08/02/2021
Date deposited: 26/07/2021
ISSN (print): 1661-6596
ISSN (electronic): 1422-0067
Publisher: MDPI AG
URL: https://doi.org/10.3390/ijms22041806
DOI: 10.3390/ijms22041806
PubMed id: 33670396
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