Details
| Original language | English |
|---|---|
| Article number | 7150 |
| Number of pages | 6 |
| Journal | International Journal of Molecular Sciences |
| Volume | 23 |
| Issue number | 13 |
| Early online date | 28 Jun 2022 |
| Publication status | Published - Jul 2022 |
Abstract
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.
Keywords
- Hsp90, molecular docking, protein microarray, thermophoresis, triiodothyronine
ASJC Scopus subject areas
- Chemical Engineering(all)
- Catalysis
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Chemistry(all)
- Spectroscopy
- Computer Science(all)
- Computer Science Applications
- Chemistry(all)
- Physical and Theoretical Chemistry
- Chemistry(all)
- Organic Chemistry
- Chemistry(all)
- Inorganic Chemistry
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In: International Journal of Molecular Sciences, Vol. 23, No. 13, 7150, 07.2022.
Research output: Contribution to journal › Short/Brief/Rapid Communication › Research › peer review
}
TY - JOUR
T1 - Triiodothyronine Acts as a Smart Influencer on Hsp90 via a Triiodothyronine Binding Site
AU - Fan, Lu
AU - Warnecke, Athanasia
AU - Weder, Julia
AU - Preller, Matthias
AU - Zeilinger, Carsten
N1 - Funding Information: 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 EXC 2177/1 “Hearing4all”.
PY - 2022/7
Y1 - 2022/7
N2 - 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.
AB - 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.
KW - Hsp90
KW - molecular docking
KW - protein microarray
KW - thermophoresis
KW - triiodothyronine
UR - http://www.scopus.com/inward/record.url?scp=85132836920&partnerID=8YFLogxK
U2 - 10.3390/ijms23137150
DO - 10.3390/ijms23137150
M3 - Short/Brief/Rapid Communication
C2 - 35806154
AN - SCOPUS:85132836920
VL - 23
JO - International Journal of Molecular Sciences
JF - International Journal of Molecular Sciences
SN - 1661-6596
IS - 13
M1 - 7150
ER -