6mg4: Difference between revisions
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<StructureSection load='6mg4' size='340' side='right'caption='[[6mg4]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='6mg4' size='340' side='right'caption='[[6mg4]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6mg4]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6mg4]] 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=6MG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MG4 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</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=6mg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mg4 OCA], [https://pdbe.org/6mg4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mg4 RCSB], [https://www.ebi.ac.uk/pdbsum/6mg4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mg4 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kelly | [[Category: Kelly JW]] | ||
[[Category: Morgan | [[Category: Morgan GJ]] | ||
[[Category: Mortenson | [[Category: Mortenson DE]] | ||
[[Category: Stanfield | [[Category: Stanfield RL]] | ||
[[Category: Wilson | [[Category: Wilson IA]] | ||
[[Category: Yan | [[Category: Yan NL]] | ||
Latest revision as of 09:31, 11 October 2023
Structure of full-length human lambda-6A light chain JTOStructure of full-length human lambda-6A light chain JTO
Structural highlights
Publication Abstract from PubMedIn Ig light-chain (LC) amyloidosis (AL), the unique antibody LC protein that is secreted by monoclonal plasma cells in each patient misfolds and/or aggregates, a process leading to organ degeneration. As a step toward developing treatments for AL patients with substantial cardiac involvement who have difficulty tolerating existing chemotherapy regimens, we introduce small-molecule kinetic stabilizers of the native dimeric structure of full-length LCs, which can slow or stop the amyloidogenicity cascade at its origin. A protease-coupled fluorescence polarization-based high-throughput screen was employed to identify small molecules that kinetically stabilize LCs. NMR and X-ray crystallographic data demonstrate that at least one structural family of hits bind at the LC-LC dimerization interface within full-length LCs, utilizing variable-domain residues that are highly conserved in most AL patients. Stopping the amyloidogenesis cascade at the beginning is a proven strategy to ameliorate postmitotic tissue degeneration. Stabilization of amyloidogenic immunoglobulin light chains by small molecules.,Morgan GJ, Yan NL, Mortenson DE, Rennella E, Blundon JM, Gwin RM, Lin CY, Stanfield RL, Brown SJ, Rosen H, Spicer TP, Fernandez-Vega V, Merlini G, Kay LE, Wilson IA, Kelly JW Proc Natl Acad Sci U S A. 2019 Apr 10. pii: 1817567116. doi:, 10.1073/pnas.1817567116. PMID:30971495[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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