2mkw
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution Structure of 6aJl2 and 6aJL2-R24G Amyloidogenics Light Chain Proteins== | |
| + | <StructureSection load='2mkw' size='340' side='right'caption='[[2mkw]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2mkw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MKW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MKW FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=2mkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mkw OCA], [https://pdbe.org/2mkw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mkw RCSB], [https://www.ebi.ac.uk/pdbsum/2mkw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mkw ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q5NV88_HUMAN Q5NV88_HUMAN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | AL amyloidosis is the most common amyloid systemic disease and it is characterized by the deposition of immunoglobulin light chain amyloid fibers in different organs, causing organ failure. The immunoglobulin light chain germinal line 6a has been observed to over-express in AL patients, moreover, it was observed that, out of these amyloidogenic proteins, 25% present a mutation of an Arg to Gly in position 24. In vitro studies have shown that this mutation produces proteins with a higher amyloid fiber propensity. It was proposed that this difference was due, in part, to the formation of a non-canonical structural element. In order to get a more detailed understanding of the structural and dynamic properties that govern the amyloid fibers formation process, we have determined the solution structure by NMR for the two constructs, showing that the difference in amyloid fibril formation is not due to sequence or structure. | ||
| - | + | Solution structure of 6aJL2 and 6aJL2-R24G amyloidogenics light chain proteins.,Maya-Martinez R, Gil-Rodriguez P, Amero C Biochem Biophys Res Commun. 2015 Jan 9;456(2):695-9. doi:, 10.1016/j.bbrc.2014.12.044. Epub 2014 Dec 16. PMID:25522882<ref>PMID:25522882</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2mkw" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Amero C]] | ||
| + | [[Category: Gil-Rodriguez PC]] | ||
| + | [[Category: Maya-Martinez RC]] | ||
Current revision
Solution Structure of 6aJl2 and 6aJL2-R24G Amyloidogenics Light Chain Proteins
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