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TitleCryo-EM Structure of the Full-length hnRNPA1 Amyloid Fibril.
Journal, issue, pagesJ Mol Biol, Vol. 435, Issue 18, Page 168211, Year 2023
Publish dateJul 20, 2023
AuthorsKartikay Sharma / Sambhasan Banerjee / Dilan Savran / Cedric Rajes / Sebastian Wiese / Amandeep Girdhar / Nadine Schwierz / Christopher Lee / James Shorter / Matthias Schmidt / Lin Guo / Marcus Fändrich /
PubMed AbstractHeterogeneous nuclear ribonucleoprotein A1 (hnRNPA1) is a multifunctional RNA-binding protein that is associated with neurodegenerative diseases, such as amyotrophic lateral sclerosis and multisystem ...Heterogeneous nuclear ribonucleoprotein A1 (hnRNPA1) is a multifunctional RNA-binding protein that is associated with neurodegenerative diseases, such as amyotrophic lateral sclerosis and multisystem proteinopathy. In this study, we have used cryo-electron microscopy to investigate the three-dimensional structure of amyloid fibrils from full-length hnRNPA1 protein. We find that the fibril core is formed by a 45-residue segment of the prion-like low-complexity domain of the protein, whereas the remaining parts of the protein (275 residues) form a fuzzy coat around the fibril core. The fibril consists of two fibril protein stacks that are arranged into a pseudo-2 screw symmetry. The ordered core harbors several of the positions that are known to be affected by disease-associated mutations, but does not encompass the most aggregation-prone segments of the protein. These data indicate that the structures of amyloid fibrils from full-length proteins may be more complex than anticipated by current theories on protein misfolding.
External linksJ Mol Biol / PubMed:37481159 / PubMed Central
MethodsEM (helical sym.)
Resolution3.32 Å
Structure data

14739

7zj2

EMDB-14739, PDB-7zj2:
Amyloid fibril (in vitro) from full-length hnRNPA1 protein
Method: EM (helical sym.) / Resolution: 3.32 Å

Source
  • homo sapiens (human)
KeywordsNUCLEAR PROTEIN / Amyloidosis / Misfolding disease / Inflammation / Prion / Protein fibril

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