6z1o
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==AL amyloid fibril from a lambda 3 light chain in conformation A== | |
| + | <StructureSection load='6z1o' size='340' side='right'caption='[[6z1o]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Z1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Z1O 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]] 3.2Å</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=6z1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6z1o OCA], [https://pdbe.org/6z1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6z1o RCSB], [https://www.ebi.ac.uk/pdbsum/6z1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6z1o ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Systemic AL amyloidosis is a debilitating and potentially fatal disease that arises from the misfolding and fibrillation of immunoglobulin light chains (LCs). The disease is patient-specific with essentially each patient possessing a unique LC sequence. In this study, we present two ex vivo fibril structures of a lambda3 LC. The fibrils were extracted from the explanted heart of a patient (FOR005) and consist of 115-residue fibril proteins, mainly from the LC variable domain. The fibril structures imply that a 180 degrees rotation around the disulfide bond and a major unfolding step are necessary for fibrils to form. The two fibril structures show highly similar fibril protein folds, differing in only a 12-residue segment. Remarkably, the two structures do not represent separate fibril morphologies, as they can co-exist at different z-axial positions within the same fibril. Our data imply the presence of structural breaks at the interface of the two structural forms. | ||
| - | + | Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis.,Radamaker L, Baur J, Huhn S, Haupt C, Hegenbart U, Schonland S, Bansal A, Schmidt M, Fandrich M Nat Commun. 2021 Feb 8;12(1):875. doi: 10.1038/s41467-021-21126-2. PMID:33558536<ref>PMID:33558536</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6z1o" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Fandrich M]] | ||
| + | [[Category: Radamaker L]] | ||
Current revision
AL amyloid fibril from a lambda 3 light chain in conformation A
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