6SDZ
transthyritin derived amyloid fibril from patient with hereditary V30M ATTR amyloidosis
Summary for 6SDZ
| Entry DOI | 10.2210/pdb6sdz/pdb |
| EMDB information | 10150 |
| Descriptor | Transthyretin (1 entity in total) |
| Functional Keywords | amyloid fibril, systemic attr amyloidosis, ex vivo, misfolding, patient tissue, transthyritin, protein fibril |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 11 |
| Total formula weight | 151903.69 |
| Authors | Fritz, G.,Agarwal, S.,Faendrich, M. (deposition date: 2019-07-29, release date: 2019-11-13, Last modification date: 2024-05-22) |
| Primary citation | Schmidt, M.,Wiese, S.,Adak, V.,Engler, J.,Agarwal, S.,Fritz, G.,Westermark, P.,Zacharias, M.,Fandrich, M. Cryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis. Nat Commun, 10:5008-5008, 2019 Cited by PubMed Abstract: 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. PubMed: 31676763DOI: 10.1038/s41467-019-13038-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.97 Å) |
Structure validation
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