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''' | ==Mcg immunoglobulin variable domain with methylene blue== | ||
<StructureSection load='5acm' size='340' side='right' caption='[[5acm]], [[Resolution|resolution]] 1.05Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5acm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ACM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ACM FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MBT:3,7-BIS(DIMETHYLAMINO)PHENOTHIAZIN-5-IUM'>MBT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5acl|5acl]]</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=5acm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5acm OCA], [http://pdbe.org/5acm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5acm RCSB], [http://www.ebi.ac.uk/pdbsum/5acm PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Overproduction of immunoglobulin light chains leads to systemic amyloidosis, a lethal disease characterized by the formation of amyloid fibrils in patients' tissues. Excess light chains are in equilibrium between dimers and less stable monomers which can undergo irreversible aggregation to the amyloid state. The dimers therefore must disassociate into monomers prior to forming amyloid fibrils. Here we identify ligands that inhibit amyloid formation by stabilizing the Mcg light chain variable domain dimer and shifting the equilibrium away from the amyloid-prone monomer. | |||
Inhibition by small-molecule ligands of formation of amyloid fibrils of an immunoglobulin light chain variable domain.,Brumshtein B, Esswein SR, Salwinski L, Phillips ML, Ly AT, Cascio D, Sawaya MR, Eisenberg DS Elife. 2015 Nov 18;4. pii: e10935. doi: 10.7554/eLife.10935. PMID:26576950<ref>PMID:26576950</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5acm" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Brumshtein, B]] | [[Category: Brumshtein, B]] | ||
[[Category: Cascio, D]] | [[Category: Cascio, D]] | ||
[[Category: Eisenberg, D S]] | |||
[[Category: Esswein, S R]] | |||
[[Category: Ly, A T]] | |||
[[Category: Phillips, M L]] | |||
[[Category: Salwinski, L]] | |||
[[Category: Sawaya, M R]] | |||
[[Category: Immune system]] | |||
[[Category: Immunoglobulin variable domain]] | |||
[[Category: Mcg]] | |||
[[Category: Methylene blue]] | |||
Revision as of 19:13, 2 December 2015
Mcg immunoglobulin variable domain with methylene blueMcg immunoglobulin variable domain with methylene blue
Structural highlights
Publication Abstract from PubMedOverproduction of immunoglobulin light chains leads to systemic amyloidosis, a lethal disease characterized by the formation of amyloid fibrils in patients' tissues. Excess light chains are in equilibrium between dimers and less stable monomers which can undergo irreversible aggregation to the amyloid state. The dimers therefore must disassociate into monomers prior to forming amyloid fibrils. Here we identify ligands that inhibit amyloid formation by stabilizing the Mcg light chain variable domain dimer and shifting the equilibrium away from the amyloid-prone monomer. Inhibition by small-molecule ligands of formation of amyloid fibrils of an immunoglobulin light chain variable domain.,Brumshtein B, Esswein SR, Salwinski L, Phillips ML, Ly AT, Cascio D, Sawaya MR, Eisenberg DS Elife. 2015 Nov 18;4. pii: e10935. doi: 10.7554/eLife.10935. PMID:26576950[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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