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The structure of the neurotoxin palytoxin determined by MicroED

Palytoxin (PTX) is a potent neurotoxin found in marine animals that can cause serious symptoms such as muscle contractions, haemolysis of red blood cells and potassium leakage. Despite years of research, very little is known about the mechanism of PTX. However, recent advances in the field of cryoEM...

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Autores principales: Gillman, Cody, Patel, Khushboo, Unge, Johan, Gonen, Tamir
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10081313/
https://www.ncbi.nlm.nih.gov/pubmed/37034718
http://dx.doi.org/10.1101/2023.03.31.535166
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author Gillman, Cody
Patel, Khushboo
Unge, Johan
Gonen, Tamir
author_facet Gillman, Cody
Patel, Khushboo
Unge, Johan
Gonen, Tamir
author_sort Gillman, Cody
collection PubMed
description Palytoxin (PTX) is a potent neurotoxin found in marine animals that can cause serious symptoms such as muscle contractions, haemolysis of red blood cells and potassium leakage. Despite years of research, very little is known about the mechanism of PTX. However, recent advances in the field of cryoEM, specifically the use of microcrystal electron diffraction (MicroED), have allowed us to determine the structure of PTX. It was discovered that PTX folds into a hairpin motif and is able to bind to the extracellular gate of Na,K-ATPase, which is responsible for maintaining the electrochemical gradient across the plasma membrane. These findings, along with molecular docking simulations, have provided important insights into the mechanism of PTX and can potentially aid in the development of molecular agents for treating cases of PTX exposure.
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spelling pubmed-100813132023-04-08 The structure of the neurotoxin palytoxin determined by MicroED Gillman, Cody Patel, Khushboo Unge, Johan Gonen, Tamir bioRxiv Article Palytoxin (PTX) is a potent neurotoxin found in marine animals that can cause serious symptoms such as muscle contractions, haemolysis of red blood cells and potassium leakage. Despite years of research, very little is known about the mechanism of PTX. However, recent advances in the field of cryoEM, specifically the use of microcrystal electron diffraction (MicroED), have allowed us to determine the structure of PTX. It was discovered that PTX folds into a hairpin motif and is able to bind to the extracellular gate of Na,K-ATPase, which is responsible for maintaining the electrochemical gradient across the plasma membrane. These findings, along with molecular docking simulations, have provided important insights into the mechanism of PTX and can potentially aid in the development of molecular agents for treating cases of PTX exposure. Cold Spring Harbor Laboratory 2023-06-01 /pmc/articles/PMC10081313/ /pubmed/37034718 http://dx.doi.org/10.1101/2023.03.31.535166 Text en https://creativecommons.org/licenses/by/4.0/This work is licensed under a Creative Commons Attribution 4.0 International License (https://creativecommons.org/licenses/by/4.0/) , which allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use.
spellingShingle Article
Gillman, Cody
Patel, Khushboo
Unge, Johan
Gonen, Tamir
The structure of the neurotoxin palytoxin determined by MicroED
title The structure of the neurotoxin palytoxin determined by MicroED
title_full The structure of the neurotoxin palytoxin determined by MicroED
title_fullStr The structure of the neurotoxin palytoxin determined by MicroED
title_full_unstemmed The structure of the neurotoxin palytoxin determined by MicroED
title_short The structure of the neurotoxin palytoxin determined by MicroED
title_sort structure of the neurotoxin palytoxin determined by microed
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10081313/
https://www.ncbi.nlm.nih.gov/pubmed/37034718
http://dx.doi.org/10.1101/2023.03.31.535166
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