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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| Format: | Article |
| Language: | English |
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Nature Publishing Group
2019-05-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-019-09923-2 |
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doaj-1f190bc76aba4d9fb248940a644fa9a92021-05-11T12:15:20ZengNature Publishing GroupNature Communications2041-17232019-05-0110111110.1038/s41467-019-09923-2Side chain to main chain hydrogen bonds stabilize a polyglutamine helix in a transcription factorAlbert Escobedo0Busra Topal1Micha B. A. Kunze2Juan Aranda3Giulio Chiesa4Daniele Mungianu5Ganeko Bernardo-Seisdedos6Bahareh Eftekharzadeh7Margarida Gairí8Roberta Pierattelli9Isabella C. Felli10Tammo Diercks11Oscar Millet12Jesús García13Modesto Orozco14Ramon Crehuet15Kresten Lindorff-Larsen16Xavier Salvatella17Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and TechnologyInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and TechnologyStructural Biology and NMR Laboratory, Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of CopenhagenInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and TechnologyInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and TechnologyInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and TechnologyCIC bioGUNEInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and TechnologyNMR Facility, Scientific and Technological Centers University of Barcelona (CCiTUB)CERM and Department of Chemistry “Ugo Schiff”, University of FlorenceCERM and Department of Chemistry “Ugo Schiff”, University of FlorenceCIC bioGUNECIC bioGUNEInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and TechnologyInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and TechnologyInstitute for Advanced Chemistry of Catalonia (IQAC-CSIC)Structural Biology and NMR Laboratory, Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of CopenhagenInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and TechnologyPolyglutamine (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.https://doi.org/10.1038/s41467-019-09923-2 |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| 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 |
| spellingShingle |
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 Nature Communications |
| 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 Publishing Group |
| series |
Nature Communications |
| issn |
2041-1723 |
| publishDate |
2019-05-01 |
| 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. |
| url |
https://doi.org/10.1038/s41467-019-09923-2 |
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