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Triiodothyronine Acts as a Smart Influencer on Hsp90 via a Triiodothyronine Binding Site

  • Microarray-based experiments revealed that thyroid hormone triiodothyronine (T3) enhanced the binding of Cy5-labeled ATP on heat shock protein 90 (Hsp90). By molecular docking experiments with T3 on Hsp90, we identified a T3 binding site (TBS) near the ATP binding site on Hsp90. A synthetic peptide encoding HHHHHHRIKEIVKKHSQFIGYPITLFVEKE derived from the TBS on Hsp90 showed, in MST experiments, the binding of T3 at an EC50 of 50 μM. The binding motif can influence the activity of Hsp90 by hindering ATP accessibility or the release of ADP.

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Document Type:Article
Author:Lu Fan, Athanasia Warnecke, Julia Weder, Matthias Preller, Carsten Zeilinger
Parent Title (English):International Journal of Molecular Sciences
Article Number:7150
Number of pages:6
Place of publication:Basel
Publishing Institution:Hochschule Bonn-Rhein-Sieg
Date of first publication:2022/06/28
Copyright:© 2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license.
Funding:Parts of the project were funded by FOR 5170: CytoLabs-Systematic Investigation and Exploitation of Cytochalasans, ZE 338/16-1. This work was supported by the DFG Cluster of Excellence EX7C 2177/1 "Hearing4all".
Keyword:HSP90; molecular docking; protein microarray; thermophoresis; triiodothyronine
Departments, institutes and facilities:Fachbereich Angewandte Naturwissenschaften
Institut für Technik, Ressourcenschonung und Energieeffizienz (TREE)
Institut für funktionale Gen-Analytik (IFGA)
Dewey Decimal Classification (DDC):5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Entry in this database:2022/07/11
Licence (German):License LogoCreative Commons - CC BY - Namensnennung 4.0 International