2rjm: Difference between revisions

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-[[Image:2rjm.jpg|left|200px]]
+{{Seed}}
+[[Image:2rjm.png|left|200px]]
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 {{STRUCTURE_2rjm|  PDB=2rjm  |  SCENE=  }}
-'''3Ig structure of titin domains I67-I69 E-to-A mutated variant'''
+===3Ig structure of titin domains I67-I69 E-to-A mutated variant===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_18212128}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18212128 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18212128}}
 ==About this Structure==
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 ==Reference==
 A regular pattern of Ig super-motifs defines segmental flexibility as the elastic mechanism of the titin chain., von Castelmur E, Marino M, Svergun DI, Kreplak L, Ucurum-Fotiadis Z, Konarev PV, Urzhumtsev A, Labeit D, Labeit S, Mayans O, Proc Natl Acad Sci U S A. 2008 Jan 29;105(4):1186-91. Epub 2008 Jan 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18212128 18212128]
+Poly-Ig tandems from I-band titin share extended domain arrangements irrespective of the distinct features of their modular constituents., Marino M, Svergun DI, Kreplak L, Konarev PV, Maco B, Labeit D, Mayans O, J Muscle Res Cell Motil. 2005;26(6-8):355-65. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16341830 16341830]
 [[Category: Non-specific serine/threonine protein kinase]]
 [[Category: Castelmur, E von.]]
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 [[Category: Structural protein]]
 [[Category: Titin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 17:02:14 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:15:26 2008''