View source for 5acl


==Mcg immunoglobulin variable domain with sulfasalazine==
<StructureSection load='5acl' size='340' side='right'caption='[[5acl]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5acl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ACL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ACL FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAS:2-HYDROXY-(5-([4-(2-PYRIDINYLAMINO)SULFONYL]PHENYL)AZO)BENZOIC+ACID'>SAS</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">[[5acm|5acm]]</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=5acl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5acl OCA], [http://pdbe.org/5acl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5acl RCSB], [http://www.ebi.ac.uk/pdbsum/5acl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5acl ProSAT]</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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5acl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Brumshtein, B]]
[[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]]