A Metastable Contact and Structural Disorder in the Estrogen Receptor Transactivation Domain

Peng, Yi; Cao, Shufen; Kiselar, Janna; Xiao, Xiangzhu; Du, Zhanwen; Hsieh, An; Ko, Soobin; Chen, Yinghua; Agrawal, Prashansa; Zheng, Wenwei; Shi, Wuxian; Jiang, Wei; Yang, Lin; Chance, Mark R.; Surewicz, Witold K.; Buck, Matthias; Yang, Sichun

doi:10.1016/j.str.2018.10.026

Title: A Metastable Contact and Structural Disorder in the Estrogen Receptor Transactivation Domain

Journal Article · Fri Feb 01 00:00:00 EST 2019 · Structure

DOI:https://doi.org/10.1016/j.str.2018.10.026· OSTI ID:1598049

Peng, Yi; Cao, Shufen; Kiselar, Janna; Xiao, Xiangzhu; Du, Zhanwen; Hsieh, An; Ko, Soobin; Chen, Yinghua; Agrawal, Prashansa; Zheng, Wenwei; Shi, Wuxian; Jiang, Wei; Yang, Lin; Chance, Mark R.; Surewicz, Witold K.; Buck, Matthias;

The N-terminal transactivation domain (NTD) of estrogen receptor alpha, a well-known member of the family of intrinsically disordered proteins, mediates the receptor's transactivation function. However, an accurate molecular dissection of NTD's structure-function relationships remains elusive. Here, we show that the NTD adopts a mostly disordered, unexpectedly compact conformation that undergoes structural expansion on chemical denaturation. By combining small-angle X-ray scattering, hydroxyl radical protein footprinting, and computational modeling, we derive the ensemble-structures of the NTD and determine its ensemble-contact map revealing metastable long-range contacts, e.g., between residues I33 and S118. We show that mutation at S118, a known phosphorylation site, promotes conformational changes and increases coactivator binding. We further demonstrate via fluorine-19 (¹⁹F) nuclear magnetic resonance that mutations near I33 alter ¹⁹F chemical shifts at S118, confirming the proposed I33-S118 contact in the ensemble of structural disorder. As a result, these findings extend our understanding of how specific contact metastability mediates critical functions of disordered proteins.

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Research Organization:: Brookhaven National Laboratory (BNL), Upton, NY (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: GM114056; AC02-98CH10886; EB009998; SC0012704

OSTI ID:: 1598049

Alternate ID(s):: OSTI ID: 1498275

Report Number(s):: BNL-211316-2019-JAAM; S0969212618303873; PII: S0969212618303873

Journal Information:: Structure, Journal Name: Structure Vol. 27 Journal Issue: 2; ISSN 0969-2126

Publisher:: ElsevierCopyright Statement

Country of Publication:: United Kingdom

Language:: English

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Cited by: 27 works

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