Synthesis and Crystal Structure of a Phosphorylated Estrogen Receptor Ligand Binding Domain

72Citations
Citations of this article
68Readers
Mendeley users who have this article in their library.
Get full text

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.

Cite

CITATION STYLE

APA

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

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free