2rjm: Difference between revisions

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-[[Image:2rjm.png|left|200px]]
-<!--
+==3Ig structure of titin domains I67-I69 E-to-A mutated variant==
-The line below this paragraph, containing "STRUCTURE_2rjm", creates the "Structure Box" on the page.
+<StructureSection load='2rjm' size='340' side='right'caption='[[2rjm]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2rjm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RJM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RJM FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
--->
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rjm OCA], [https://pdbe.org/2rjm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rjm RCSB], [https://www.ebi.ac.uk/pdbsum/2rjm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rjm ProSAT]</span></td></tr>
-{{STRUCTURE_2rjm|  PDB=2rjm  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/O97791_RABIT O97791_RABIT]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rj/2rjm_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2rjm ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===3Ig structure of titin domains I67-I69 E-to-A mutated variant===
+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:18212128<ref>PMID:18212128</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_18212128}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2rjm" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 18212128 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_18212128}}
-==About this Structure==
-[[2rjm]] is a 1 chain structure of [[Titin]] with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RJM OCA].
 ==See Also==
-*[[Titin]]
+*[[Titin 3D structures|Titin 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:18212128</ref><ref group="xtra">PMID:16341830</ref><references group="xtra"/>
+__TOC__
-[[Category: Non-specific serine/threonine protein kinase]]
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Oryctolagus cuniculus]]
-[[Category: Castelmur, E von.]]
+[[Category: Labeit D]]
-[[Category: Labeit, D.]]
+[[Category: Labeit S]]
-[[Category: Labeit, S.]]
+[[Category: Marino M]]
-[[Category: Marino, M.]]
+[[Category: Mayans O]]
-[[Category: Mayans, O.]]
+[[Category: Von Castelmur E]]
-[[Category: Extended poly-ig filament]]
-[[Category: Ig i-set]]
-[[Category: Structural protein]]
-[[Category: Titin]]