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-Structure paper
タイトル | Common transthyretin-derived amyloid fibril structures in patients with hereditary ATTR amyloidosis. |
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ジャーナル・号・ページ | Nat Commun, Vol. 14, Issue 1, Page 7623, Year 2023 |
掲載日 | 2023年11月22日 |
著者 | Maximilian Steinebrei / Julian Baur / Anaviggha Pradhan / Niklas Kupfer / Sebastian Wiese / Ute Hegenbart / Stefan O Schönland / Matthias Schmidt / Marcus Fändrich / |
PubMed 要旨 | Systemic ATTR amyloidosis is an increasingly important protein misfolding disease that is provoked by the formation of amyloid fibrils from transthyretin protein. The pathological and clinical ...Systemic ATTR amyloidosis is an increasingly important protein misfolding disease that is provoked by the formation of amyloid fibrils from transthyretin protein. The pathological and clinical disease manifestations and the number of pathogenic mutational changes in transthyretin are highly diverse, raising the question whether the different mutations may lead to different fibril morphologies. Using cryo-electron microscopy, however, we show here that the fibril structure is remarkably similar in patients that are affected by different mutations. Our data suggest that the circumstances under which these fibrils are formed and deposited inside the body - and not only the fibril morphology - are crucial for defining the phenotypic variability in many patients. |
リンク | Nat Commun / PubMed:37993462 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 2.3673 - 3.39 Å |
構造データ | EMDB-17736, PDB-8pke: EMDB-17737, PDB-8pkf: EMDB-17738, PDB-8pkg: |
由来 |
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キーワード | PROTEIN FIBRIL / Transthyretin / ATTR amyloidosis / ATTRV20I / amyloid fibril / misfolding disease / cryo-EM / ATTRG47E / ATTRV122I |