6hud: Difference between revisions
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6hud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hud OCA], [http://pdbe.org/6hud PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hud RCSB], [http://www.ebi.ac.uk/pdbsum/6hud PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hud ProSAT]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6hud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hud OCA], [http://pdbe.org/6hud PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hud RCSB], [http://www.ebi.ac.uk/pdbsum/6hud PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hud ProSAT]</span></td></tr> | ||
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== Publication Abstract from PubMed == | |||
Systemic light chain amyloidosis (AL) is a life-threatening disease caused by aggregation and deposition of monoclonal immunoglobulin light chains (LC) in target organs. Severity of heart involvement is the most important factor determining prognosis. Here, we report the 4.0 A resolution cryo-electron microscopy map and molecular model of amyloid fibrils extracted from the heart of an AL amyloidosis patient with severe amyloid cardiomyopathy. The helical fibrils are composed of a single protofilament, showing typical 4.9 A stacking and cross-beta architecture. Two distinct polypeptide stretches (total of 77 residues) from the LC variable domain (Vl) fit the fibril density. Despite Vl high sequence variability, residues stabilizing the fibril core are conserved through different cardiotoxic Vl, highlighting structural motifs that may be common to misfolding-prone LCs. Our data shed light on the architecture of LC amyloids, correlate amino acid sequences with fibril assembly, providing the grounds for development of innovative medicines. | |||
Cryo-EM structure of cardiac amyloid fibrils from an immunoglobulin light chain AL amyloidosis patient.,Swuec P, Lavatelli F, Tasaki M, Paissoni C, Rognoni P, Maritan M, Brambilla F, Milani P, Mauri P, Camilloni C, Palladini G, Merlini G, Ricagno S, Bolognesi M Nat Commun. 2019 Mar 20;10(1):1269. doi: 10.1038/s41467-019-09133-w. PMID:30894521<ref>PMID:30894521</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 6hud" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||
Revision as of 11:17, 3 April 2019
Cryo-EM structure of cardiac amyloid fibrils from an immunoglobulin light chain (AL) amyloidosis patient.Cryo-EM structure of cardiac amyloid fibrils from an immunoglobulin light chain (AL) amyloidosis patient.
Structural highlights
Publication Abstract from PubMedSystemic light chain amyloidosis (AL) is a life-threatening disease caused by aggregation and deposition of monoclonal immunoglobulin light chains (LC) in target organs. Severity of heart involvement is the most important factor determining prognosis. Here, we report the 4.0 A resolution cryo-electron microscopy map and molecular model of amyloid fibrils extracted from the heart of an AL amyloidosis patient with severe amyloid cardiomyopathy. The helical fibrils are composed of a single protofilament, showing typical 4.9 A stacking and cross-beta architecture. Two distinct polypeptide stretches (total of 77 residues) from the LC variable domain (Vl) fit the fibril density. Despite Vl high sequence variability, residues stabilizing the fibril core are conserved through different cardiotoxic Vl, highlighting structural motifs that may be common to misfolding-prone LCs. Our data shed light on the architecture of LC amyloids, correlate amino acid sequences with fibril assembly, providing the grounds for development of innovative medicines. Cryo-EM structure of cardiac amyloid fibrils from an immunoglobulin light chain AL amyloidosis patient.,Swuec P, Lavatelli F, Tasaki M, Paissoni C, Rognoni P, Maritan M, Brambilla F, Milani P, Mauri P, Camilloni C, Palladini G, Merlini G, Ricagno S, Bolognesi M Nat Commun. 2019 Mar 20;10(1):1269. doi: 10.1038/s41467-019-09133-w. PMID:30894521[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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