The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294
Open accessAbstract
Histone lysine methylation is an important epigenetic mark that regulates gene expression and chromatin organization. G9a and G9a-like protein (GLP) are euchromatin-associated methyltransferases that repress transcription by methylating histone H3 Lys9. BIX-01294 was originally identified as a G9a inhibitor during a chemical library screen of small molecules and has previously been used in the generation of induced pluripotent stem cells. Here we present the crystal structure of the catalytic SET domain of GLP in complex with BIX-01294 and S-adenosyl-L-homocysteine. The inhibitor is bound in the substrate peptide groove at the location where the histone H3 residues N-terminal to the target lysine lie in the previously solved structure of the complex with histone peptide. The inhibitor resembles the bound conformation of histone H3 Lys4 to Arg8, and is positioned in place by residues specific for G9a and GLP through specific interactions.
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Takahashi, K., & Yamanaka, S. (2006) · Cell · doi:10.1016/j.cell.2006.07.024 · Cited by 26,673
Friesner, R. A., Banks, J. L., Murphy, R. B., Halgren, T. A., Klicic, J. J., Mainz, D. T., Repasky, M. P., Knoll, E. H., Shelley, M., Perry, J. K., et al. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm0306430 · Cited by 10,057
Protein lysine methyltransferase G9a acts on non-histone targets
Rathert, P., Dhayalan, A., Murakami, M., Zhang, X., Tamas, R., Jurkowska, R., Komatsu, Y., Shinkai, Y., Cheng, X., & Jeltsch, A. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.88 · Cited by 347
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Cited by
Epigenetic protein families: a new frontier for drug discovery
Arrowsmith, C. H., Bountra, C., Fish, P. V., Lee, K., & Schapira, M. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3674 · Cited by 1,327
Essential Role of the Histone Methyltransferase G9a in Cocaine-Induced Plasticity
Maze, I., Covington, H. E., Dietz, D. M., LaPlant, Q., Renthal, W., Russo, S. J., Mechanic, M., Mouzon, E., Neve, R. L., Haggarty, S. J., et al. (2010) · Science · doi:10.1126/science.1179438 · Cited by 665
H3K9 methyltransferase G9a and the related molecule GLP
Shinkai, Y., & Tachibana, M. (2011) · Genes & Development · doi:10.1101/gad.2027411 · Cited by 558
A chemical probe selectively inhibits G9a and GLP methyltransferase activity in cells
Vedadi, M., Barsyte-Lovejoy, D., Liu, F., Rival-Gervier, S., Allali-Hassani, A., Labrie, V., Wigle, T. J., DiMaggio, P. A., Wasney, G. A., Siarheyeva, A., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.599 · Cited by 527
Critical roles of non-histone protein lysine methylation in human tumorigenesis
Hamamoto, R., Saloura, V., & Nakamura, Y. (2015) · Nature Reviews Cancer · doi:10.1038/nrc3884 · Cited by 376
Metadata
- Authors
- Chang, Y., Zhang, X., Horton, J. R., Upadhyay, A. K., Spannhoff, A., Liu, J., Snyder, J. P., Bedford, M. T., & Cheng, X.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2009-02-15
- Volume
- 16
- Issue
- 3
- Pages
- 312-317
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2033027341
- Cited by
- 308
- References
- 3
- FWCI
- 10.08
- Type
- journal article
- Language
- en
- Open access
- green
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- Chang, Y., Zhang, X., Horton, J. R., Upadhyay, A. K., Spannhoff, A., Liu, J., Snyder, J. P., Bedford, M. T., & Cheng, X. (2009). Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294. Nature Structural & Molecular Biology. https://doi.org/10.1038/nsmb.1560
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