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Synthesis and Crystal Structure of a Phosphorylated Estrogen Receptor Ligand Binding Domain
Author(s) -
Möcklinghoff Sabine,
Rose Rolf,
Carraz Maëlle,
Visser Arie,
Ottmann Christian,
Brunsveld Luc
Publication year - 2010
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201000532
Subject(s) - phosphorylation , estrogen receptor , chemistry , ligand (biochemistry) , estrogen , domain (mathematical analysis) , estrogen related receptor gamma , receptor , microbiology and biotechnology , biochemistry , computational biology , biophysics , stereochemistry , biology , nuclear receptor , endocrinology , genetics , transcription factor , gene , cancer , breast cancer , mathematical analysis , mathematics
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).
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