8ADE

Wild type ATTR amyloid fibril from senile systemic amyloidosis

「7Z40」から置き換えられました

8ADE の概要

• エントリーDOI: 10.2210/pdb8ade/pdb
• EMDBエントリー: 15361
• 分子名称: Transthyretin (1 entity in total)
• 機能のキーワード: transthyretin amyliod fibril, protein fibril
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 96441.52

構造登録者

Schmidt, M.,Steinebrei, M. (登録日: 2022-07-08, 公開日: 2022-11-23, 最終更新日: 2024-07-24)

主引用文献

Steinebrei, M.,Gottwald, J.,Baur, J.,Rocken, C.,Hegenbart, U.,Schonland, S.,Schmidt, M.
Cryo-EM structure of an ATTRwt amyloid fibril from systemic non-hereditary transthyretin amyloidosis.
Nat Commun, 13:6398-6398, 2022

PubMed Abstract: Wild type transthyretin-derived amyloid (ATTRwt) is the major component of non-hereditary transthyretin amyloidosis. Its accumulation in the heart of elderly patients is life threatening. A variety of genetic variants of transthyretin can lead to hereditary transthyretin amyloidosis, which shows different clinical symptoms, like age of onset and pattern of organ involvement. However, in the case of non-hereditary transthyretin amyloidosis ATTRwt fibril deposits are located primarily in heart tissue. In this structural study we analyzed ATTRwt amyloid fibrils from the heart of a patient with non-hereditary transthyretin amyloidosis. We present a 2.78 Å reconstructed density map of these ATTRwt fibrils using cryo electron microscopy and compare it with previously published V30M variants of ATTR fibrils extracted from heart and eye of different patients. All structures show a remarkably similar spearhead like shape in their cross section, formed by the same N- and C-terminal fragments of transthyretin with some minor differences. This demonstrates common features for ATTR fibrils despite differences in mutations and patients.

PubMed: 36302762
DOI: 10.1038/s41467-022-33591-4

実験手法

ELECTRON MICROSCOPY (2.78 Å)