View source for 9liy


==The cryo-EM structure of amyloid fibrils from abdominal fat of an AL amyloidosis patient (case 2) - polymorph 2.==
<StructureSection load='9liy' size='340' side='right'caption='[[9liy]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9liy]] 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=9LIY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9LIY 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]] 3.2&#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=9liy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9liy OCA], [https://pdbe.org/9liy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9liy RCSB], [https://www.ebi.ac.uk/pdbsum/9liy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9liy ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Systemic light chain amyloidosis (AL) is characterized by amyloid fibril deposition in multiple organs, often severely affecting cardiac function. In this study, we extracted amyloid fibrils directly from abdominal fat and cardiac tissue biopsies obtained from three AL patients. Using cryo-electron microscopy, we determined five distinct structures of light chain (LC) amyloid fibrils. Our results demonstrate that LC fibrils from different patients adopt unique structural conformations, highlighting patient-specific fibril variations. Conversely, LC fibrils extracted from different tissues within the same patient share highly similar overall fibril structures, yet exhibit localized conformational variations, potentially shaped by distinct environmental cofactors. This study emphasizes the combined roles of patient-specific protein sequences and tissue-specific microenvironments in defining LC fibril conformation. The determination of LC fibril structures directly from easily accessible abdominal fat biopsy provides critical molecular insights into AL amyloidosis pathology, facilitating the development of therapeutic strategies.

Biopsy-resolved cryo-EM structures of amyloid fibrils provide molecular insights into AL amyloidosis.,Yao Y, Zhao Q, Yao S, Xu Y, Liu K, Cao T, Sun B, Zhou J, Liu C, Li D Proc Natl Acad Sci U S A. 2026 Jan 13;123(2):e2515454123. doi: , 10.1073/pnas.2515454123. Epub 2026 Jan 6. PMID:41493812<ref>PMID:41493812</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9liy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Li D]]
[[Category: Liu C]]
[[Category: Yao YX]]
[[Category: Zhao QY]]