Synthesis and crystal structure of phosphorylated estrogen receptor ligand binding domain

S. Möcklinghoff, R. Rose, M. Carraz, A. Visser, C. Ottmann, L. Brunsveld

Research output: Contribution to journalArticleAcademicpeer-review

43 Citations (Scopus)
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Abstract

Chemical protein synthesis allows the generation of milligram quantities of correctly folded and previously inaccessible tyrosine-phosphorylated estrogen receptor a (ERa) and ß (ERß) ligand binding domains. By using this synthetic strategy, the crystal structure of a post-translationally modified nuclear receptor (pY488 ERß) could be obtained for the first time
Original languageEnglish
Pages (from-to)2251-2254
JournalChemBioChem
Volume11
Issue number16
DOIs
Publication statusPublished - 2010

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