6SDZ

transthyritin derived amyloid fibril from patient with hereditary V30M ATTR amyloidosis

6SDZ の概要

• エントリーDOI: 10.2210/pdb6sdz/pdb
• EMDBエントリー: 10150
• 分子名称: Transthyretin (1 entity in total)
• 機能のキーワード: amyloid fibril, systemic attr amyloidosis, ex vivo, misfolding, patient tissue, transthyritin, protein fibril
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 11
• 化学式量合計: 151903.69

構造登録者

Fritz, G.,Agarwal, S.,Faendrich, M. (登録日: 2019-07-29, 公開日: 2019-11-13, 最終更新日: 2024-05-22)

主引用文献

Schmidt, M.,Wiese, S.,Adak, V.,Engler, J.,Agarwal, S.,Fritz, G.,Westermark, P.,Zacharias, M.,Fandrich, M.
Cryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis.
Nat Commun, 10:5008-5008, 2019

PubMed Abstract: ATTR amyloidosis is one of the worldwide most abundant forms of systemic amyloidosis. The disease is caused by the misfolding of transthyretin protein and the formation of amyloid deposits at different sites within the body. Here, we present a 2.97 Å cryo electron microscopy structure of a fibril purified from the tissue of a patient with hereditary Val30Met ATTR amyloidosis. The fibril consists of a single protofilament that is formed from an N-terminal and a C-terminal fragment of transthyretin. Our structure provides insights into the mechanism of misfolding and implies the formation of an early fibril state from unfolded transthyretin molecules, which upon proteolysis converts into mature ATTR amyloid fibrils.

PubMed: 31676763
DOI: 10.1038/s41467-019-13038-z

実験手法

ELECTRON MICROSCOPY (2.97 Å)