Summary information and primary citation
- PDB-id
-
9hxv;
DSSR-derived features in text and
JSON formats
- Class
- oxidoreductase
- Method
- X-ray (1.9 Å)
- Summary
- Crystal structure of tet2-DNA in complex with iox1
- Reference
-
Willems S, Maksumic L, Niggenaber J, Lin TC, Schulz T,
Weisner J, Sievers S, Muller MP, Summerer D, Rauh D
(2025): "Advancing
TET Inhibitor Development: From Structural Insights to
Biological Evaluation." Acs Med.Chem.Lett.,
16, 804-810. doi: 10.1021/acsmedchemlett.5c00042.
- Abstract
- Ten-eleven translocation (TET) methylcytosine
dioxygenases are part of the epigenetic regulatory
machinery that erases DNA methylation. Aberrant TET
activities are frequently found in hematopoietic
malignancies, where loss of TET2 function leads to DNA
hypermethylation. A comprehensive understanding of the
biological role of TETs is essential to elucidate disease
pathogenesis and identify novel therapeutic strategies. We
present a robust pipeline integrating protein X-ray
crystallography, molecular modeling, and pharmacophore
analysis to advance the current TET inhibitor development.
In addition, we have synthesized and evaluated a series of
8-hydroxyquinoline (8-HQ) derivatives, demonstrating their
potential as chemical tools to explore TET function
further. These findings lay the groundwork for a
TET-centered therapeutic approach.
