2MKW

Solution Structure of 6aJl2 and 6aJL2-R24G Amyloidogenics Light Chain Proteins

2MKW の概要

• エントリーDOI: 10.2210/pdb2mkw/pdb
• 関連するPDBエントリー: 2W0K
• NMR情報: BMRB: 19798
• 分子名称: V1-22 protein (1 entity in total)
• 機能のキーワード: light chain, amyloidosis, systemic, lambda, immune system
• 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: 11861.77

構造登録者

Amero, C.,Maya-Martinez, R.C.,Gil-Rodriguez, P.C. (登録日: 2014-02-13, 公開日: 2014-06-18, 最終更新日: 2024-11-06)

主引用文献

Maya-Martinez, R.,Gil-Rodriguez, P.,Amero, C.
Solution structure of 6aJL2 and 6aJL2-R24G amyloidogenics light chain proteins.
Biochem.Biophys.Res.Commun., 456:695-699, 2015

PubMed Abstract: AL amyloidosis is the most common amyloid systemic disease and it is characterized by the deposition of immunoglobulin light chain amyloid fibers in different organs, causing organ failure. The immunoglobulin light chain germinal line 6a has been observed to over-express in AL patients, moreover, it was observed that, out of these amyloidogenic proteins, 25% present a mutation of an Arg to Gly in position 24. In vitro studies have shown that this mutation produces proteins with a higher amyloid fiber propensity. It was proposed that this difference was due, in part, to the formation of a non-canonical structural element. In order to get a more detailed understanding of the structural and dynamic properties that govern the amyloid fibers formation process, we have determined the solution structure by NMR for the two constructs, showing that the difference in amyloid fibril formation is not due to sequence or structure.

PubMed: 25522882
DOI: 10.1016/j.bbrc.2014.12.044

実験手法

SOLUTION NMR