@article{046e3cbbb56e4fad8e9e283b35099b77,
title = "A Metastable Contact and Structural Disorder in the Estrogen Receptor Transactivation Domain",
abstract = "We unraveled that the transactivation domain of estrogen receptor is structurally disordered, yet unexpectedly compact, and that a metastable Ile33-Ser118 contact is observed to inhibit coactivator binding. Disruption by mutagenesis alters ensemble-structures and coactivator binding, providing a functional link of oncogenic Ser118 phosphorylation in breast cancer endocrine resistance.",
keywords = "SAXS, contact metastability, intrinsically disordered protein, multi-technique data integration, protein footprinting, structural disorder",
author = "Yi Peng and Shufen Cao and Janna Kiselar and Xiangzhu Xiao and Zhanwen Du and An Hsieh and Soobin Ko and Yinghua Chen and Prashansa Agrawal and Wenwei Zheng and Wuxian Shi and Wei Jiang and Lin Yang and Chance, {Mark R.} and Surewicz, {Witold K.} and Matthias Buck and Sichun Yang",
note = "Funding Information: We thank Sayan Gupta for assistance with footprinting experiments, Geof Greene for inspiration of this project, Marc Parisien for constructive comments, and Liang-Yuan Chiu and Hao Ruan for assistance with 19 F NMR experiments. We also thank anonymous reviewers for constructive suggestions. The work of S.Y. was supported by an NIH grant ( GM114056 ). Use of the synchrotron sources was supported by the U.S. Department of Energy ( DE-AC02-98CH10886 ) and by NIH ( EB009998 ). Publisher Copyright: {\textcopyright} 2018 Elsevier Ltd",
year = "2019",
month = feb,
day = "5",
doi = "10.1016/j.str.2018.10.026",
language = "English (US)",
volume = "27",
pages = "229--240.e4",
journal = "Structure",
issn = "0969-2126",
publisher = "Cell Press",
number = "2",
}