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==Crystal structure of an amyloidogenic light chain dimer H7==
<StructureSection load='5muh' size='340' side='right'caption='[[5muh]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5muh]] is a 2 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=5MUH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MUH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65&#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=5muh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5muh OCA], [https://pdbe.org/5muh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5muh RCSB], [https://www.ebi.ac.uk/pdbsum/5muh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5muh ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Light chain amyloidosis (AL), the most common systemic amyloidosis, is caused by the overproduction and the aggregation of monoclonal immunoglobulin light chains (LC) in target organs. Due to genetic rearrangement and somatic hypermutation, virtually, each AL patient presents a different amyloidogenic LC. Because of such complexity, the fine molecular determinants of LC aggregation propensity and proteotoxicity are, to date, unclear; significantly, their decoding requires investigating large sets of cases. Aiming to achieve generalizable observations, we systematically characterised a pool of thirteen sequence-diverse full length LCs. Eight amyloidogenic LCs were selected as responsible for severe cardiac symptoms in patients; five non-amyloidogenic LCs were isolated from patients affected by multiple myeloma. Our comprehensive approach (consisting of spectroscopic techniques, limited proteolysis, and X-ray crystallography) shows that low fold stability and high protein dynamics correlate with amyloidogenic LCs, while hydrophobicity, structural rearrangements and nature of the LC dimeric association interface (as observed in seven crystal structures here presented) do not appear to play a significant role in defining amyloid propensity. Based on the structural and biophysical data, our results highlight shared properties driving LC amyloid propensity, and these data will be instrumental for the design of synthetic inhibitors of LC aggregation.

Concurrent structural and biophysical traits link with immunoglobulin light chains amyloid propensity.,Oberti L, Rognoni P, Barbiroli A, Lavatelli F, Russo R, Maritan M, Palladini G, Bolognesi M, Merlini G, Ricagno S Sci Rep. 2017 Dec 1;7(1):16809. doi: 10.1038/s41598-017-16953-7. PMID:29196671<ref>PMID:29196671</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bacarizo J]]
[[Category: Bolognesi M]]
[[Category: Maritan M]]
[[Category: Oberti L]]
[[Category: Ricagno S]]
[[Category: Rognoni P]]
[[Category: Russo R]]