5ACL

Mcg immunoglobulin variable domain with sulfasalazine

Summary for 5ACL

• Entry DOI: 10.2210/pdb5acl/pdb
• Related: 5ACM
• Descriptor: MCG, 2-HYDROXY-(5-([4-(2-PYRIDINYLAMINO)SULFONYL]PHENYL)AZO)BENZOIC ACID, SULFATE ION, ... (4 entities in total)
• Functional Keywords: immune system, mcg, immunoglobulin variable domain, methylene blue
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Secreted : P01709
• Total number of polymer chains: 1
• Total formula weight: 12059.97

Authors

Brumshtein, B.,Esswein, S.R.,Salwinski, L.,Phillips, M.L.,Ly, A.T.,Cascio, D.,Sawaya, M.R.,Eisenberg, D.S. (deposition date: 2015-08-17, release date: 2015-12-02, Last modification date: 2024-11-13)

Primary citation

Brumshtein, B.,Esswein, S.R.,Salwinski, L.,Phillips, M.L.,Ly, A.T.,Cascio, D.,Sawaya, M.R.,Eisenberg, D.S.
Inhibition by small-molecule ligands of formation of amyloid fibrils of an immunoglobulin light chain variable domain.
Elife, 4:e10935-e10935, 2015

PubMed Abstract: 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.

PubMed: 26576950
DOI: 10.7554/eLife.10935

Experimental method

X-RAY DIFFRACTION (1.49 Å)