Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Brumshtein B, Esswein SR, Salwinski L, Phillips ML, Ly AT, Cascio D, Sawaya MR, Eisenberg DS. Inhibition by small-molecule ligands of formation of amyloid fibrils of an immunoglobulin light chain variable domain. Elife. 2015 Nov 18;4. pii: e10935. doi: 10.7554/eLife.10935. PMID:26576950 doi:http://dx.doi.org/10.7554/eLife.10935
