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Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids
Ulm Univ, Inst Prot Biochem, D-89081 Ulm, Germany.ORCID-id: 0000-0002-1557-2621
Howard Hughes Med Inst, Janelia Res Campus, Ashburn, VA 20147 USA.ORCID-id: 0000-0002-1731-516X
Ulm Univ, Inst Prot Biochem, D-89081 Ulm, Germany.
Martin Luther Univ Halle Wittenberg, Inst Biochem & Biotechnol, D-06120 Halle, Saale, Germany.
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2019 (engelsk)Inngår i: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 10, artikkel-id 1104Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Systemic AA amyloidosis is a worldwide occurring protein misfolding disease of humans and animals. It arises from the formation of amyloid fibrils from the acute phase protein serum amyloid A. Here, we report the purification and electron cryo-microscopy analysis of amyloid fibrils from a mouse and a human patient with systemic AA amyloidosis. The obtained resolutions are 3.0 angstrom and 2.7 angstrom for the murine and human fibril, respectively. The two fibrils differ in fundamental properties, such as presence of right-hand or left-hand twisted cross-beta sheets and overall fold of the fibril proteins. Yet, both proteins adopt highly similar beta-arch conformations within the N-terminal similar to 21 residues. Our data demonstrate the importance of the fibril protein N-terminus for the stability of the analyzed amyloid fibril morphologies and suggest strategies of combating this disease by interfering with specific fibril polymorphs.

sted, utgiver, år, opplag, sider
NATURE PUBLISHING GROUP , 2019. Vol. 10, artikkel-id 1104
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Patologi
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URN: urn:nbn:se:uu:diva-379892DOI: 10.1038/s41467-019-09033-zISI: 000460510000001PubMedID: 30846696OAI: oai:DiVA.org:uu-379892DiVA, id: diva2:1298597
Forskningsfinansiär
EU, Horizon 2020German Research Foundation (DFG), FA 456/15-1German Research Foundation (DFG), SCHM 3276/1Tilgjengelig fra: 2019-03-25 Laget: 2019-03-25 Sist oppdatert: 2019-03-29bibliografisk kontrollert

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