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TitleCryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis.
Journal, issue, pagesNat Commun, Vol. 10, Issue 1, Page 5008, Year 2019
Publish dateNov 1, 2019
AuthorsMatthias Schmidt / Sebastian Wiese / Volkan Adak / Jonas Engler / Shubhangi Agarwal / Günter Fritz / Per Westermark / Martin Zacharias / Marcus Fändrich /
PubMed AbstractATTR 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 ...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 Å 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.
External linksNat Commun / PubMed:31676763 / PubMed Central
MethodsEM (helical sym.)
Resolution2.97 Å
Structure data

10150

6sdz

EMDB-10150, PDB-6sdz:
transthyritin derived amyloid fibril from patient with hereditary V30M ATTR amyloidosis
Method: EM (helical sym.) / Resolution: 2.97 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / amyloid fibril / systemic ATTR amyloidosis / ex vivo / misfolding / patient tissue / transthyritin

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