Abstract
Chemical protein synthesis allows the generation of milligram quantities of correctly folded and previously inaccessible tyrosine phosphorylated estrogen receptor α (ERα) and β (ERβ) ligand binding domains. By using this synthetic strategy, the crystal structure of a post-translationally modified nuclear receptor (pY488 ERβ) could be obtained for the first time (see figure). Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
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Möcklinghoff, S., Rose, R., Carraz, M., Visser, A., Ottmann, C., & Brunsveld, L. (2010). Synthesis and Crystal Structure of a Phosphorylated Estrogen Receptor Ligand Binding Domain. ChemBioChem, 11(16), 2251–2254. https://doi.org/10.1002/cbic.201000532
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