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7U11

TMEM106B(120-254) protofilament from frontotemporal lobar degeneration with TDP-43 pathology (FTLD-TDP) type A (case 1)

Summary for 7U11
Entry DOI10.2210/pdb7u11/pdb
EMDB information26268 26273 26274 26275 26276
DescriptorTransmembrane protein 106B, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
Functional Keywordstmem106b, amyloid fibril, protein fibril
Biological sourceHomo sapiens (human)
Total number of polymer chains3
Total formula weight49162.54
Authors
Primary citationChang, A.,Xiang, X.,Wang, J.,Lee, C.,Arakhamia, T.,Simjanoska, M.,Wang, C.,Carlomagno, Y.,Zhang, G.,Dhingra, S.,Thierry, M.,Perneel, J.,Heeman, B.,Forgrave, L.M.,DeTure, M.,DeMarco, M.L.,Cook, C.N.,Rademakers, R.,Dickson, D.W.,Petrucelli, L.,Stowell, M.H.B.,Mackenzie, I.R.A.,Fitzpatrick, A.W.P.
Homotypic fibrillization of TMEM106B across diverse neurodegenerative diseases.
Cell, 185:1346-1355.e15, 2022
Cited by
PubMed Abstract: Misfolding and aggregation of disease-specific proteins, resulting in the formation of filamentous cellular inclusions, is a hallmark of neurodegenerative disease with characteristic filament structures, or conformers, defining each proteinopathy. Here we show that a previously unsolved amyloid fibril composed of a 135 amino acid C-terminal fragment of TMEM106B is a common finding in distinct human neurodegenerative diseases, including cases characterized by abnormal aggregation of TDP-43, tau, or α-synuclein protein. A combination of cryoelectron microscopy and mass spectrometry was used to solve the structures of TMEM106B fibrils at a resolution of 2.7 Å from postmortem human brain tissue afflicted with frontotemporal lobar degeneration with TDP-43 pathology (FTLD-TDP, n = 8), progressive supranuclear palsy (PSP, n = 2), or dementia with Lewy bodies (DLB, n = 1). The commonality of abundant amyloid fibrils composed of TMEM106B, a lysosomal/endosomal protein, to a broad range of debilitating human disorders indicates a shared fibrillization pathway that may initiate or accelerate neurodegeneration.
PubMed: 35247328
DOI: 10.1016/j.cell.2022.02.026
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.2 Å)
Structure validation

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건을2024-10-30부터공개중

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