8PKG

ATTRV122I amyloid fibril from hereditary ATTR amloidosis

8PKG の概要

• エントリーDOI: 10.2210/pdb8pkg/pdb
• EMDBエントリー: 17738
• 分子名称: Transthyretin (1 entity in total)
• 機能のキーワード: transthyretin, attr amyloidosis, attrv122i, amyloid fibril, misfolding disease, cryo-em, protein fibril
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 82748.32

構造登録者

Steinebrei, M.,Schmidt, M.,Faendrich, M. (登録日: 2023-06-26, 公開日: 2023-12-06)

主引用文献

Steinebrei, M.,Baur, J.,Pradhan, A.,Kupfer, N.,Wiese, S.,Hegenbart, U.,Schonland, S.O.,Schmidt, M.,Fandrich, M.
Common transthyretin-derived amyloid fibril structures in patients with hereditary ATTR amyloidosis.
Nat Commun, 14:7623-7623, 2023

PubMed Abstract: Systemic ATTR amyloidosis is an increasingly important protein misfolding disease that is provoked by the formation of amyloid fibrils from transthyretin protein. The pathological and clinical disease manifestations and the number of pathogenic mutational changes in transthyretin are highly diverse, raising the question whether the different mutations may lead to different fibril morphologies. Using cryo-electron microscopy, however, we show here that the fibril structure is remarkably similar in patients that are affected by different mutations. Our data suggest that the circumstances under which these fibrils are formed and deposited inside the body - and not only the fibril morphology - are crucial for defining the phenotypic variability in many patients.

PubMed: 37993462
DOI: 10.1038/s41467-023-43301-3

実験手法

ELECTRON MICROSCOPY (2.99 Å)