9BYN

Cryo-EM structure of amyloid fibril extracted from nerve of a variant ATTR V30M amyloidosis patient

9BYN の概要

• エントリーDOI: 10.2210/pdb9byn/pdb
• EMDBエントリー: 45039
• 分子名称: Transthyretin (1 entity in total)
• 機能のキーワード: amyloidosis, systemic amyloidosis, attr, nerve, protein fibril
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 69047.13

構造登録者

Nguyen, A.B.,Afrin, S.,Yakubovska, A.,Saelices, L. (登録日: 2024-05-23, 公開日: 2025-03-12)

主引用文献

Nguyen, B.A.,Afrin, S.,Yakubovska, A.,Singh, V.,Pedretti, R.,Bassett, P.,Pekala, M.,Alicea, J.V.,Kunach, P.,Wang, L.,Lemoff, A.,Kluve-Beckerman, B.,Saelices, L.
ATTRv-V30M amyloid fibrils from heart and nerves exhibit structural homogeneity.
Structure, 32:2244-2250.e3, 2024

PubMed Abstract: Amyloidogenic transthyretin (ATTR) amyloidosis is a systemic disease characterized by the deposition of amyloid fibrils made of transthyretin. Transthyretin is primarily produced in tetrameric form by the liver, but also by retinal epithelium and choroid plexus. The deposition of these fibrils in the myocardium and peripheral nerves causes cardiomyopathies and neuropathies, respectively. Using cryoelectron microscopy (cryo-EM), we investigated fibrils extracted from cardiac and nerve tissues of an ATTRv-V30M patient. We found consistent fibril structures from both tissues, similar to cardiac fibrils previously described, but different from vitreous humor fibrils of the same genotype. Our findings, along with previous ATTR fibrils structural studies, suggest a uniform fibrillar architecture across different tissues when transthyretin originates from the liver. This study advances our understanding of how deposition and production sites influence fibril structure in ATTRv-V30M amyloidosis.

PubMed: 39423808
DOI: 10.1016/j.str.2024.09.021

実験手法

ELECTRON MICROSCOPY (3.36 Å)