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dc.contributor.authorSeppälä, Jonne
dc.contributor.authorTossavainen, Helena
dc.contributor.authorRodic, Nebojsa
dc.contributor.authorPermi, Perttu
dc.contributor.authorPentikäinen, Ulla
dc.contributor.authorYlänne, Jari
dc.date.accessioned2015-09-15T11:28:39Z
dc.date.available2015-09-15T11:28:39Z
dc.date.issued2015
dc.identifier.citationSeppälä, J., Tossavainen, H., Rodic, N., Permi, P., Pentikäinen, U., & Ylänne, J. (2015). Flexible Structure of Peptide-Bound Filamin A Mechanosensor Domain Pair 20–21. <i>PLoS ONE</i>, <i>10</i>(8), Article e0136969. <a href="https://doi.org/10.1371/journal.pone.0136969" target="_blank">https://doi.org/10.1371/journal.pone.0136969</a>
dc.identifier.otherCONVID_24869841
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/46821
dc.description.abstractFilamins (FLNs) are large, multidomain actin cross-linking proteins with diverse functions. Besides regulating the actin cytoskeleton, they serve as important links between the extracellular matrix and the cytoskeleton by binding cell surface receptors, functioning as scaffolds for signaling proteins, and binding several other cytoskeletal proteins that regulate cell adhesion dynamics. Structurally, FLNs are formed of an amino terminal actin-binding domain followed by 24 immunoglobulin-like domains (IgFLNs). Recent studies have demonstrated that myosin-mediated contractile forces can reveal hidden protein binding sites in the domain pairs IgFLNa18–19 and 20–21, enabling FLNs to transduce mechanical signals in cells. The atomic structures of these mechanosensor domain pairs in the resting state are known, as well as the structures of individual IgFLN21 with ligand peptides. However, little experimental data is available on how interacting protein binding deforms the domain pair structures. Here, using small-angle x-ray scattering-based modelling, x-ray crystallography, and NMR, we show that the adaptor protein migfilin-derived peptide-bound structure of IgFLNa20–21 is flexible and adopts distinctive conformations depending on the presence or absence of the interacting peptide. The conformational changes reported here may be common for all peptides and may play a role in the mechanosensor function of the site.fi
dc.language.isoeng
dc.publisherPublic Library of Science
dc.relation.ispartofseriesPLoS ONE
dc.subject.otherfilaminsfi
dc.subject.otherpeptidesfi
dc.titleFlexible Structure of Peptide-Bound Filamin A Mechanosensor Domain Pair 20–21
dc.typeresearch article
dc.identifier.urnURN:NBN:fi:jyu-201509112851
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.updated2015-09-11T15:15:03Z
dc.type.coarhttp://purl.org/coar/resource_type/c_2df8fbb1
dc.description.reviewstatuspeerReviewed
dc.relation.issn1932-6203
dc.relation.numberinseries8
dc.relation.volume10
dc.type.versionpublishedVersion
dc.rights.copyright© 2015 Seppälä et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
dc.rights.accesslevelopenAccessfi
dc.type.publicationarticle
dc.subject.ysofilamiinit
dc.subject.ysopeptidit
jyx.subject.urihttp://www.yso.fi/onto/yso/p25674
jyx.subject.urihttp://www.yso.fi/onto/yso/p15258
dc.rights.urlhttp://creativecommons.org/licenses/by/4.0/
dc.relation.doi10.1371/journal.pone.0136969
dc.type.okmA1


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© 2015 Seppälä et al. This is an open
access article distributed under the terms of the
Creative Commons Attribution License, which permits
unrestricted use, distribution, and reproduction in any
medium, provided the original author and source are
credited.
Except where otherwise noted, this item's license is described as © 2015 Seppälä et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.