Side chain to main chain hydrogen bonds stabilize a polyglutamine helix in a transcription factor
Polyglutamine (polyQ) tracts are low-complexity regions and their expansion is linked to certain neurodegenerative diseases. Here the authors combine experimental and computational approaches to find that the length of the androgen receptor polyQ tract correlates with its helicity and show that the...
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Nature Portfolio
2019
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oai:doaj.org-article:1f190bc76aba4d9fb248940a644fa9a92021-12-02T15:35:39ZSide chain to main chain hydrogen bonds stabilize a polyglutamine helix in a transcription factor10.1038/s41467-019-09923-22041-1723https://doaj.org/article/1f190bc76aba4d9fb248940a644fa9a92019-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-09923-2https://doaj.org/toc/2041-1723Polyglutamine (polyQ) tracts are low-complexity regions and their expansion is linked to certain neurodegenerative diseases. Here the authors combine experimental and computational approaches to find that the length of the androgen receptor polyQ tract correlates with its helicity and show that the polyQ helical structure is stabilized by hydrogen bonds between the Gln side chains and main chain carbonyl groups.Albert EscobedoBusra TopalMicha B. A. KunzeJuan ArandaGiulio ChiesaDaniele MungianuGaneko Bernardo-SeisdedosBahareh EftekharzadehMargarida GairíRoberta PierattelliIsabella C. FelliTammo DiercksOscar MilletJesús GarcíaModesto OrozcoRamon CrehuetKresten Lindorff-LarsenXavier SalvatellaNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-11 (2019) |
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Science Q Albert Escobedo Busra Topal Micha B. A. Kunze Juan Aranda Giulio Chiesa Daniele Mungianu Ganeko Bernardo-Seisdedos Bahareh Eftekharzadeh Margarida Gairí Roberta Pierattelli Isabella C. Felli Tammo Diercks Oscar Millet Jesús García Modesto Orozco Ramon Crehuet Kresten Lindorff-Larsen Xavier Salvatella Side chain to main chain hydrogen bonds stabilize a polyglutamine helix in a transcription factor |
description |
Polyglutamine (polyQ) tracts are low-complexity regions and their expansion is linked to certain neurodegenerative diseases. Here the authors combine experimental and computational approaches to find that the length of the androgen receptor polyQ tract correlates with its helicity and show that the polyQ helical structure is stabilized by hydrogen bonds between the Gln side chains and main chain carbonyl groups. |
format |
article |
author |
Albert Escobedo Busra Topal Micha B. A. Kunze Juan Aranda Giulio Chiesa Daniele Mungianu Ganeko Bernardo-Seisdedos Bahareh Eftekharzadeh Margarida Gairí Roberta Pierattelli Isabella C. Felli Tammo Diercks Oscar Millet Jesús García Modesto Orozco Ramon Crehuet Kresten Lindorff-Larsen Xavier Salvatella |
author_facet |
Albert Escobedo Busra Topal Micha B. A. Kunze Juan Aranda Giulio Chiesa Daniele Mungianu Ganeko Bernardo-Seisdedos Bahareh Eftekharzadeh Margarida Gairí Roberta Pierattelli Isabella C. Felli Tammo Diercks Oscar Millet Jesús García Modesto Orozco Ramon Crehuet Kresten Lindorff-Larsen Xavier Salvatella |
author_sort |
Albert Escobedo |
title |
Side chain to main chain hydrogen bonds stabilize a polyglutamine helix in a transcription factor |
title_short |
Side chain to main chain hydrogen bonds stabilize a polyglutamine helix in a transcription factor |
title_full |
Side chain to main chain hydrogen bonds stabilize a polyglutamine helix in a transcription factor |
title_fullStr |
Side chain to main chain hydrogen bonds stabilize a polyglutamine helix in a transcription factor |
title_full_unstemmed |
Side chain to main chain hydrogen bonds stabilize a polyglutamine helix in a transcription factor |
title_sort |
side chain to main chain hydrogen bonds stabilize a polyglutamine helix in a transcription factor |
publisher |
Nature Portfolio |
publishDate |
2019 |
url |
https://doaj.org/article/1f190bc76aba4d9fb248940a644fa9a9 |
work_keys_str_mv |
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