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Cryo-EM structures of human PRMT5:MEP50 complex reveal chemical basis for designing high-specificity inhibitors
Published online by Cambridge University Press: 30 July 2021
Abstract
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- Type
- Cryo-EM in Drug Discovery
- Information
- Copyright
- Copyright © The Author(s), 2021. Published by Cambridge University Press on behalf of the Microscopy Society of America
References
Afonine, P.V., Poon, B.K., Read, R.J., Sobolev, O.V., Terwilliger, T.C., Urzhumtsev, A., and Adams, P.D. (2018). Real-space refinement in PHENIX for cryo-EM and crystallography. Acta Crystallogr D Struct Biol 74, 531-544.CrossRefGoogle ScholarPubMed
Alinari, L., Mahasenan, K.V., Yan, F., Karkhanis, V., Chung, J.H., Smith, E.M., Quinion, C., Smith, P.L., Kim, L., Patton, J.T., et al. (2015). Selective inhibition of protein arginine methyltransferase 5 blocks initiation and maintenance of B-cell transformation. Blood 125, 2530-2543.CrossRefGoogle ScholarPubMed
Andreu-Perez, P., Esteve-Puig, R., de Torre-Minguela, C., Lopez-Fauqued, M., Bech-Serra, J.J., Tenbaum, S., Garcia-Trevijano, E.R., Canals, F., Merlino, G., Avila, M.A., et al. (2011). Protein arginine methyltransferase 5 regulates ERK1/2 signal transduction amplitude and cell fate through CRAF. Sci Signal 4, ra58.CrossRefGoogle ScholarPubMed
Antonysamy, S., Bonday, Z., Campbell, R.M., Doyle, B., Druzina, Z., Gheyi, T., Han, B., Jungheim, L.N., Qian, Y., Rauch, C., et al. (2012). Crystal structure of the human PRMT5:MEP50 complex. Proc Natl Acad Sci U S A 109, 17960-17965.CrossRefGoogle ScholarPubMed
Banasavadi-Siddegowda, Y.K., Welker, A.M., An, M., Yang, X., Zhou, W., Shi, G., Imitola, J., Li, C., Hsu, S., Wang, J., et al. (2018). PRMT5 as a druggable target for glioblastoma therapy. Neuro Oncol 20, 753-763.CrossRefGoogle ScholarPubMed
Biggar, K.K., and Li, S.S. (2015). Non-histone protein methylation as a regulator of cellular signalling and function. Nat Rev Mol Cell Biol 16, 5-17.CrossRefGoogle ScholarPubMed
Burgos, E.S., Wilczek, C., Onikubo, T., Bonanno, J.B., Jansong, J., Reimer, U., and Shechter, D. (2015). Histone H2A and H4 N-terminal tails are positioned by the MEP50 WD repeat protein for efficient methylation by the PRMT5 arginine methyltransferase. J Biol Chem 290, 9674-9689.Google ScholarPubMed
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