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000141075 0247_ $$2doi$$a10.1371/journal.pbio.1001261
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000141075 1001_ $$aPinotsis, N.
000141075 1101_ $$aDESY$$bEuropean Molecular Biology Laboratory
000141075 245__ $$aSuperhelical architecture of the myosin filament-linking protein myomesin with unusual elastic properties
000141075 260__ $$aLawrence, KS$$bPLoS$$c2012
000141075 300__ $$ae1001261
000141075 3367_ $$00$$2EndNote$$aJournal Article
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000141075 3367_ $$2BibTeX$$aARTICLE
000141075 440_0 $$0PERI:(DE-600)2126773-X$$aPLoS Biol$$v10$$x1544-9173$$y2
000141075 500__ $$3Converted on 2013-05-30 09:52
000141075 500__ $$3Converted on 2013-06-21 19:21
000141075 520__ $$aActive muscles generate substantial mechanical forces by the contraction/relaxation cycle, and, to maintain an ordered state, they require molecular structures of extraordinary stability. These forces are sensed and buffered by unusually long and elastic filament proteins with highly repetitive domain arrays. Members of the myomesin protein family function as molecular bridges that connect major filament systems in the central M-band of muscle sarcomeres, which is a central locus of passive stress sensing. To unravel the mechanism of molecular elasticity in such filament-connecting proteins, we have determined the overall architecture of the complete C-terminal immunoglobulin domain array of myomesin by X-ray crystallography, electron microscopy, solution X-ray scattering, and atomic force microscopy. Our data reveal a dimeric tail-to-tail filament structure of about 360 Å in length, which is folded into an irregular superhelical coil arrangement of almost identical α-helix/domain modules. The myomesin filament can be stretched to about 2.5-fold its original length by reversible unfolding of these linkers, a mechanism that to our knowledge has not been observed previously. Our data explain how myomesin could act as a highly elastic ribbon to maintain the overall structural organization of the sarcomeric M-band. In general terms, our data demonstrate how repetitive domain modules such as those found in myomesin could generate highly elastic protein structures in highly organized cell systems such as muscle sarcomeres.
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000141075 588__ $$aDataset connected to Pubmed
000141075 650_7 $$00$$2NLM Chemicals$$aMuscle Proteins
000141075 650_7 $$00$$2NLM Chemicals$$amyomesin
000141075 650_2 $$2MeSH$$aCrystallography, X-Ray
000141075 650_2 $$2MeSH$$aElasticity
000141075 650_2 $$2MeSH$$aMicroscopy, Atomic Force
000141075 650_2 $$2MeSH$$aMicroscopy, Electron, Transmission
000141075 650_2 $$2MeSH$$aModels, Molecular
000141075 650_2 $$2MeSH$$aMuscle Proteins: chemistry
000141075 650_2 $$2MeSH$$aMuscle Proteins: ultrastructure
000141075 650_2 $$2MeSH$$aProtein Structure, Quaternary
000141075 650_2 $$2MeSH$$aProtein Structure, Secondary
000141075 650_2 $$2MeSH$$aProtein Structure, Tertiary
000141075 650_2 $$2MeSH$$aSarcomeres: chemistry
000141075 650_2 $$2MeSH$$aScattering, Small Angle
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000141075 7001_ $$aChatziefthimiou, S. D.
000141075 7001_ $$aBerkemeier, F.
000141075 7001_ $$aBeuron, F.
000141075 7001_ $$aMavridis, I. M.
000141075 7001_ $$aKonarev, P. V.
000141075 7001_ $$aSvergun, D. I.
000141075 7001_ $$aMorris, E.
000141075 7001_ $$aRief, M.
000141075 7001_ $$aWilmanns, M.
000141075 773__ $$0PERI:(DE-600)2126773-X$$a10.1371/journal.pbio.1001261$$gVol. 10, p. e1001261$$pe1001261$$q10<e1001261$$tPLoS biology$$v10$$x1544-9173$$y2012
000141075 85640 $$uhttp://www.plosbiology.org/article/info%3Adoi%2F10.1371%2Fjournal.pbio.1001261
000141075 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3279516
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000141075 9141_ $$a(c) Public Library of Science$$y2012
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