4UNV
Covalent dimer of lambda variable domains
Summary for 4UNV
| Entry DOI | 10.2210/pdb4unv/pdb |
| Related | 4UNT 4UNU |
| Descriptor | IG LAMBDA CHAIN V-II REGION MGC, SULFATE ION (3 entities in total) |
| Functional Keywords | immune system, bence-jones, immunoglobulin, amyloid |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 1 |
| Total formula weight | 11745.67 |
| Authors | Brumshtein, B.,Esswein, S.,Landau, M.,Ryan, C.,Whitelegge, J.,Sawaya, M.,Eisenberg, D.S. (deposition date: 2014-05-30, release date: 2014-08-27, Last modification date: 2024-11-13) |
| Primary citation | Brumshtein, B.,Esswein, S.R.,Landau, M.,Ryan, C.M.,Whitelegge, J.P.,Phillips, M.L.,Cascio, D.,Sawaya, M.R.,Eisenberg, D.S. Formation of Amyloid Fibers by Monomeric Light-Chain Variable Domains. J.Biol.Chem., 289:27513-, 2014 Cited by PubMed Abstract: Systemic light chain amyloidosis is a lethal disease characterized by excess immunoglobulin light chains and light chain fragments composed of variable domains, which aggregate into amyloid fibers. These fibers accumulate and damage organs. Some light chains induce formation of amyloid fibers, whereas others do not, making it unclear what distinguishes amyloid formers from non-formers. One mechanism by which sequence variation may reduce propensity to form amyloid fibers is by shifting the equilibrium toward an amyloid-resistant quaternary structure. Here we identify the monomeric form of the Mcg immunoglobulin light chain variable domain as the quaternary unit required for amyloid fiber assembly. Dimers of Mcg variable domains remain stable and soluble, yet become prone to assemble into amyloid fibers upon disassociation into monomers. PubMed: 25138218DOI: 10.1074/JBC.M114.585638 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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