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dc.contributor.author
Vijayvargia, Ravi
dc.contributor.author
Epand, Raquel F.
dc.contributor.author
Leitner, Alexander
dc.contributor.author
Jung, Tae-Yang
dc.contributor.author
Shin, Baehyun
dc.contributor.author
Jung, Roy
dc.contributor.author
Lloret, Alejandro
dc.contributor.author
Atwal, Randy S.
dc.contributor.author
Lee, Hyeongseok
dc.contributor.author
Lee, Jong-Min
dc.contributor.author
Aebersold, Ruedi
dc.contributor.author
Hebert, Hans
dc.contributor.author
Song, Ji-Joon
dc.contributor.author
Seong, Ihn Sik
dc.date.accessioned
2018-09-10T15:33:45Z
dc.date.available
2017-06-12T03:55:30Z
dc.date.available
2018-09-10T15:33:45Z
dc.date.issued
2016
dc.identifier.other
10.7554/eLife.11184
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/114979
dc.identifier.doi
10.3929/ethz-b-000114979
dc.description.abstract
The polyglutamine expansion in huntingtin protein causes Huntington’s disease. Here, we investigated structural and biochemical properties of huntingtin and the effect of the polyglutamine expansion using various biophysical experiments including circular dichroism, single-particle electron microscopy and cross-linking mass spectrometry. Huntingtin is likely composed of five distinct domains and adopts a spherical α-helical solenoid where the amino-terminal and carboxyl-terminal regions fold to contain a circumscribed central cavity. Interestingly, we showed that the polyglutamine expansion increases α-helical properties of huntingtin and affects the intramolecular interactions among the domains. Our work delineates the structural characteristics of full-length huntingtin, which are affected by the polyglutamine expansion, and provides an elegant solution to the apparent conundrum of how the extreme amino-terminal polyglutamine tract confers a novel property on huntingtin, causing the disease.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
eLife Sciences Publications
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.title
Huntingtin's spherical solenoid structure enables polyglutamine tract-dependent modulation of its structure and function
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
ethz.journal.title
eLife
ethz.journal.volume
5
en_US
ethz.pages.start
e11184
en_US
ethz.size
16 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.identifier.nebis
007613147
ethz.publication.place
Cambridge
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02538 - Institut für Molekulare Systembiologie / Institute for Molecular Systems Biology::03663 - Aebersold, Rudolf / Aebersold, Rudolf
en_US
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02538 - Institut für Molekulare Systembiologie / Institute for Molecular Systems Biology::03663 - Aebersold, Rudolf / Aebersold, Rudolf
ethz.date.deposited
2017-06-12T03:59:11Z
ethz.source
ECIT
ethz.identifier.importid
imp5936544a2a86b77602
ethz.ecitpid
pub:176789
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2017-07-17T11:02:22Z
ethz.rosetta.lastUpdated
2018-09-10T15:33:52Z
ethz.rosetta.exportRequired
true
ethz.rosetta.versionExported
true
ethz.COinS
ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.atitle=Huntingtin's%20spherical%20solenoid%20structure%20enables%20polyglutamine%20tract-dependent%20modulation%20of%20its%20structure%20and%20function&rft.jtitle=eLife&rft.date=2016&rft.volume=5&rft.spage=e11184&rft.au=Vijayvargia,%20Ravi&Epand,%20Raquel%20F.&Leitner,%20Alexander&Jung,%20Tae-Yang&Shin,%20Baehyun&rft.genre=article&
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