4UNV

Covalent dimer of lambda variable domains

4UNV の概要

• エントリーDOI: 10.2210/pdb4unv/pdb
• 関連するPDBエントリー: 4UNT 4UNU
• 分子名称: IG LAMBDA CHAIN V-II REGION MGC, SULFATE ION (3 entities in total)
• 機能のキーワード: immune system, bence-jones, immunoglobulin, amyloid
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11745.67

構造登録者

Brumshtein, B.,Esswein, S.,Landau, M.,Ryan, C.,Whitelegge, J.,Sawaya, M.,Eisenberg, D.S. (登録日: 2014-05-30, 公開日: 2014-08-27, 最終更新日: 2024-11-13)

主引用文献

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

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: 25138218
DOI: 10.1074/JBC.M114.585638

実験手法

X-RAY DIFFRACTION (1.6 Å)