Synthesis and crystal structure of phosphorylated estrogen receptor ligand binding domain

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

doi:10.1002/cbic.201000532

Synthesis and crystal structure of phosphorylated estrogen receptor ligand binding domain

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

Chemical Biology

Research output: Contribution to journal › Article › Academic › peer-review

45 Citations (Scopus)

2 Downloads (Pure)

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 language	English
Pages (from-to)	2251-2254
Journal	ChemBioChem
Volume	11
Issue number	16
DOIs	https://doi.org/10.1002/cbic.201000532
Publication status	Published - 2010

Access to Document

10.1002/cbic.201000532

Cite this

@article{cdf836a96d56426893df4831d8343f47,

title = "Synthesis and crystal structure of phosphorylated estrogen receptor ligand binding domain",

abstract = "Chemical protein synthesis allows the generation of milligram quantities of correctly folded and previously inaccessible tyrosine-phosphorylated estrogen receptor a (ERa) and {\ss} (ER{\ss}) ligand binding domains. By using this synthetic strategy, the crystal structure of a post-translationally modified nuclear receptor (pY488 ER{\ss}) could be obtained for the first time",

author = "S. M{\"o}cklinghoff and R. Rose and M. Carraz and A. Visser and C. Ottmann and L. Brunsveld",

year = "2010",

doi = "10.1002/cbic.201000532",

language = "English",

volume = "11",

pages = "2251--2254",

journal = "ChemBioChem",

issn = "1439-4227",

publisher = "Wiley-VCH Verlag",

number = "16",

}

TY - JOUR

T1 - Synthesis and crystal structure of phosphorylated estrogen receptor ligand binding domain

AU - Möcklinghoff, S.

AU - Rose, R.

AU - Carraz, M.

AU - Visser, A.

AU - Ottmann, C.

AU - Brunsveld, L.

PY - 2010

Y1 - 2010

N2 - 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

AB - 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

U2 - 10.1002/cbic.201000532

DO - 10.1002/cbic.201000532

M3 - Article

C2 - 20922740

VL - 11

SP - 2251

EP - 2254

JO - ChemBioChem

JF - ChemBioChem

SN - 1439-4227

IS - 16

ER -

Synthesis and crystal structure of phosphorylated estrogen receptor ligand binding domain

Abstract

Access to Document

Fingerprint

Cite this