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Article

Atomic structures of FUS LC domain segments reveal bases for reversible amyloid fibril formation.

Nature structural & molecular biology - 1 Apr 2018

Luo Feng, Gui Xinrui, Zhou Heng, Gu Jinge, Li Yichen, Liu Xiangyu, Zhao Minglei, Li Dan, Li Xueming, Liu Cong

Abstract excerpt

Thermostable cross-β structures are characteristic of pathological amyloid fibrils, but these structures cannot explain the reversible nature of fibrils formed by RNA-binding proteins such as fused in sarcoma (FUS), involved in RNA granule assembly. Here, we find that two tandem (S/G)Y(S/G) motifs of the human FUS low-complexity domain (FUS LC) form reversible fibrils in a temperature- and...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 29610493
DOI: 10.1038/s41594-018-0050-8

Genes

FUS
RAC1
RAC2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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