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Synthesis and crystal structure of a phosphorylated estrogen receptor ligand binding domain
- Source :
- ChemBioChem, 11(16), 2251-2254. Wiley-VCH Verlag
- Publication Year :
- 2010
-
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
- Subjects :
- Stereochemistry
Molecular Sequence Data
Estrogen receptor
Crystallography, X-Ray
Ligands
Biochemistry
HORMONE
PROTEINE
PHOSPHATE
Enzyme-linked receptor
Estrogen Receptor beta
5-HT5A receptor
Amino Acid Sequence
SUBSTANCE CRISTALLISEE
Phosphorylation
SYNTHESE
PHOSPHORYLATION
Molecular Biology
Estrogen receptor beta
Nuclear receptor co-repressor 1
Chemistry
Organic Chemistry
Estrogen Receptor alpha
STRUCTURE CHIMIQUE
Protein Structure, Tertiary
Nuclear receptor
ETUDE EXPERIMENTALE
Molecular Medicine
CHROMATOGRAPHIE
Estrogen-related receptor gamma
SPECTROMETRIE DE MASSE
Peptides
Estrogen receptor alpha
Protein Binding
Subjects
Details
- ISSN :
- 14397633 and 14394227
- Volume :
- 11
- Issue :
- 16
- Database :
- OpenAIRE
- Journal :
- Chembiochem : a European journal of chemical biology
- Accession number :
- edsair.doi.dedup.....9dbe7be2cac33272b3ae33e37520f01f