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Cryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis
Ulm Univ, Inst Prot Biochem, D-89081 Ulm, Germany.
Ulm Univ, Core Unit Mass Spectrometry & Prote, D-89081 Ulm, Germany.
Ulm Univ, Inst Prot Biochem, D-89081 Ulm, Germany.
Ulm Univ, Inst Prot Biochem, D-89081 Ulm, Germany.
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2019 (English)In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 10, article id 5008Article in journal (Refereed) Published
Abstract [en]

ATTR amyloidosis is one of the worldwide most abundant forms of systemic amyloidosis. The disease is caused by the misfolding of transthyretin protein and the formation of amyloid deposits at different sites within the body. Here, we present a 2.97 angstrom cryo electron microscopy structure of a fibril purified from the tissue of a patient with hereditary Val30Met ATTR amyloidosis. The fibril consists of a single protofilament that is formed from an N-terminal and a C-terminal fragment of transthyretin. Our structure provides insights into the mechanism of misfolding and implies the formation of an early fibril state from unfolded transthyretin molecules, which upon proteolysis converts into mature ATTR amyloid fibrils.

Place, publisher, year, edition, pages
NATURE PUBLISHING GROUP , 2019. Vol. 10, article id 5008
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
URN: urn:nbn:se:uu:diva-397799DOI: 10.1038/s41467-019-13038-zISI: 000493712700001PubMedID: 31676763OAI: oai:DiVA.org:uu-397799DiVA, id: diva2:1373382
Funder
German Research Foundation (DFG), SCHM 3276/1Erik, Karin och Gösta Selanders FoundationAvailable from: 2019-11-27 Created: 2019-11-27 Last updated: 2019-11-27Bibliographically approved

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