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Sökning: id:"swepub:oai:DiVA.org:liu-143657" > A regular pattern o...

  • von Castelmur, EleonoreDivision of Structural Biology, Biozentrum, University of Basel, Basel, Switzerland (författare)

A regular pattern of Ig super-motifs defines segmental flexibility as the elastic mechanism of the titin chain

  • Artikel/kapitelEngelska2008

Förlag, utgivningsår, omfång ...

  • 2008-01-29
  • Washington, DC, United States :National Academy of Sciences,2008
  • printrdacarrier

Nummerbeteckningar

  • LIBRIS-ID:oai:DiVA.org:liu-143657
  • https://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-143657URI
  • https://doi.org/10.1073/pnas.0707163105DOI

Kompletterande språkuppgifter

  • Språk:engelska
  • Sammanfattning på:engelska

Ingår i deldatabas

Klassifikation

  • Ämneskategori:ref swepub-contenttype
  • Ämneskategori:art swepub-publicationtype

Anmärkningar

  • Myofibril elasticity, critical to muscle function, is dictated by the intrasarcomeric filament titin, which acts as a molecular spring. To date, the molecular events underlying the mechanics of the folded titin chain remain largely unknown. We have elucidated the crystal structure of the 6-Ig fragment I65-I70 from the elastic I-band fraction of titin and validated its conformation in solution using small angle x-ray scattering. The long-range properties of the chain have been visualized by electron microscopy on a 19-Ig fragment and modeled for the full skeletal tandem. Results show that conserved Ig-Ig transition motifs generate high-order in the structure of the filament, where conformationally stiff segments interspersed with pliant hinges form a regular pattern of dynamic super-motifs leading to segmental flexibility in the chain. Pliant hinges support molecular shape rearrangements that dominate chain behavior at moderate stretch, whereas stiffer segments predictably oppose high stretch forces upon full chain extension. There, librational entropy can be expected to act as an energy barrier to prevent Ig unfolding while, instead, triggering the unraveling of flanking springs formed by proline, glutamate, valine, and lysine (PEVK) sequences. We propose a mechanistic model based on freely jointed rigid segments that rationalizes the response to stretch of titin Ig-tandems according to molecular features.

Ämnesord och genrebeteckningar

Biuppslag (personer, institutioner, konferenser, titlar ...)

  • Marino, MarcoDivision of Structural Biology, Biozentrum, University of Basel, Basel, Switzerland (författare)
  • Svergun, Dmitri IEuropean Molecular Biology Laboratory, Hamburg Outstation, c/o Deutsches Elektronen Synchrotron (DESY), Hamburg, Germany; Institute of Crystallography, Russian Academy of Sciences, Moscow, Russia (författare)
  • Kreplak, LaurentM. E. Müller Institute for Structural Biology, Biozentrum, University of Basel, Basel, Switzerland (författare)
  • Ucurum-Fotiadis, ZöhreDivision of Structural Biology, Biozentrum, University of Basel, Basel, Switzerland (författare)
  • Konarev, Petr VEuropean Molecular Biology Laboratory, Hamburg Outstation, c/o Deutsches Elektronen Synchrotron (DESY), Hamburg, Germany; Institute of Crystallography, Russian Academy of Sciences, Moscow, Russia (författare)
  • Urzhumtsev, AlexandreUniversity-Nancy, Vandoeuvre-les-Nancy, France; Institut de Génétique et de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique-Institut National de la Santé et de la Recherche Médicale-Université Louis Pasteur, Illkirch, France (författare)
  • Labeit, DietmarInstitut für Anästhesiologie und Operative Intensivmedizin, Universitätsklinikum Mannheim, Mannheim, Germany (författare)
  • Labeit, SiegfriedInstitut für Anästhesiologie und Operative Intensivmedizin, Universitätsklinikum Mannheim, Mannheim, Germany (författare)
  • Mayans, OlgaDivision of Structural Biology, Biozentrum, University of Basel, Basel, Switzerland; Institut für Anästhesiologie und Operative Intensivmedizin, Universitätsklinikum Mannheim, Mannheim, Germany (författare)
  • Division of Structural Biology, Biozentrum, University of Basel, Basel, SwitzerlandEuropean Molecular Biology Laboratory, Hamburg Outstation, c/o Deutsches Elektronen Synchrotron (DESY), Hamburg, Germany; Institute of Crystallography, Russian Academy of Sciences, Moscow, Russia (creator_code:org_t)

Sammanhörande titlar

  • Ingår i:Proceedings of the National Academy of Sciences of the United States of AmericaWashington, DC, United States : National Academy of Sciences105:4, s. 1186-11910027-84241091-6490

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