9eme
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==AL amyloid fibril from the FOR103 light chain== | |
| + | <StructureSection load='9eme' size='340' side='right'caption='[[9eme]], [[Resolution|resolution]] 2.92Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9eme]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9EME OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9EME FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.92Å</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=9eme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9eme OCA], [https://pdbe.org/9eme PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9eme RCSB], [https://www.ebi.ac.uk/pdbsum/9eme PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9eme ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Systemic AL amyloidosis is one of the most frequently diagnosed forms of systemic amyloidosis. It arises from mutational changes in immunoglobulin light chains. To explore whether these mutations may affect the structure of the formed fibrils, we determine and compare the fibril structures from several patients with cardiac AL amyloidosis. All patients are affected by light chains that contain an IGLV3-19 gene segment, and the deposited fibrils differ by the mutations within this common germ line background. Using cryo-electron microscopy, we here find different fibril structures in each patient. These data establish that the mutations of amyloidogenic light chains contribute to defining the fibril architecture and hence the structure of the pathogenic agent. | ||
| - | + | Light chain mutations contribute to defining the fibril morphology in systemic AL amyloidosis.,Karimi-Farsijani S, Pfeiffer PB, Banerjee S, Baur J, Kuhn L, Kupfer N, Hegenbart U, Schonland SO, Wiese S, Haupt C, Schmidt M, Fandrich M Nat Commun. 2024 Jun 15;15(1):5121. doi: 10.1038/s41467-024-49520-6. PMID:38879609<ref>PMID:38879609</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 9eme" style="background-color:#fffaf0;"></div> |
| - | [[Category: Karimi-Farsijani | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Faendrich M]] | ||
| + | [[Category: Karimi-Farsijani S]] | ||
| + | [[Category: Kupfer N]] | ||
| + | [[Category: Pfeiffer PB]] | ||
| + | [[Category: Schmidt M]] | ||
Current revision
AL amyloid fibril from the FOR103 light chain
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