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dc.contributor.authorSethi, Ritika
dc.contributor.authorYlänne, Jari
dc.date.accessioned2016-06-14T06:57:01Z
dc.date.available2016-06-14T06:57:01Z
dc.date.issued2014
dc.identifier.citationSethi, R., & Ylänne, J. (2014). Small-angle X-ray scattering reveals compact domain-domain interactions in the n-terminal region of filamin C. <i>PLoS ONE</i>, <i>9</i>(9), Article e107457. <a href="https://doi.org/10.1371/journal.pone.0107457" target="_blank">https://doi.org/10.1371/journal.pone.0107457</a>
dc.identifier.otherCONVID_23890167
dc.identifier.otherTUTKAID_63109
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/50295
dc.description.abstractFilamins are multi-domain, actin cross-linking, and scaffolding proteins. In addition to the actin cross-linking function, filamins have a role in mechanosensor signaling. The mechanosensor function is mediated by domain-domain interaction in the C-terminal region of filamins. Recently, we have shown that there is a three-domain interaction module in the Nterminal region of filamins, where the neighboring domains stabilize the structure of the middle domain and thereby regulate its interaction with ligands. In this study, we have used small-angle X-ray scattering as a tool to screen for potential domain-domain interactions in the N-terminal region. We found evidence of four domain-domain interactions with varying flexibility. These results confirm our previous study showing that domains 3, 4, and 5 exist as a compact three domain module. In addition, we report interactions between domains 11–12 and 14–15, which are thus new candidate sites for mechanical regulation.
dc.language.isoeng
dc.publisherPublic Library of Science
dc.relation.ispartofseriesPLoS ONE
dc.subject.othersmall-angle X-ray scattering
dc.subject.othercompact domain-domain interactions
dc.subject.otherfilamin C
dc.titleSmall-angle X-ray scattering reveals compact domain-domain interactions in the n-terminal region of filamin C
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-201606143068
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosDepartment of Biological and Environmental Scienceen
dc.contributor.oppiaineSolu- ja molekyylibiologiafi
dc.contributor.oppiaineNanoscience Centerfi
dc.contributor.oppiaineCell and Molecular Biologyen
dc.contributor.oppiaineNanoscience Centeren
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.date.updated2016-06-14T06:15:39Z
dc.type.coarjournal article
dc.description.reviewstatuspeerReviewed
dc.relation.issn1932-6203
dc.relation.numberinseries9
dc.relation.volume9
dc.type.versionpublishedVersion
dc.rights.copyright© 2014 Sethi, Ylänne. This is an open-access article distributed under the terms of the Creative Commons Attribution License.
dc.rights.accesslevelopenAccessfi
dc.rights.urlhttp://creativecommons.org/licenses/by/4.0/
dc.relation.doi10.1371/journal.pone.0107457


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© 2014 Sethi, Ylänne. This is an open-access article distributed under the terms of the Creative Commons Attribution License.
Except where otherwise noted, this item's license is described as © 2014 Sethi, Ylänne. This is an open-access article distributed under the terms of the Creative Commons Attribution License.