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- PDB-7qvf: TMEM106B filaments with Fold I-d from Multiple system atrophy (ca... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7qvf | ||||||
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Title | TMEM106B filaments with Fold I-d from Multiple system atrophy (case 18) | ||||||
![]() | Transmembrane protein 106B![]() | ||||||
![]() | PROTEIN FIBRIL / ![]() ![]() ![]() ![]() | ||||||
Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Lovestam, S. / Schweighauser, M. / Scheres, S.H.W. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Age-dependent formation of TMEM106B amyloid filaments in human brains. Authors: Manuel Schweighauser / Diana Arseni / Mehtap Bacioglu / Melissa Huang / Sofia Lövestam / Yang Shi / Yang Yang / Wenjuan Zhang / Abhay Kotecha / Holly J Garringer / Ruben Vidal / Grace I ...Authors: Manuel Schweighauser / Diana Arseni / Mehtap Bacioglu / Melissa Huang / Sofia Lövestam / Yang Shi / Yang Yang / Wenjuan Zhang / Abhay Kotecha / Holly J Garringer / Ruben Vidal / Grace I Hallinan / Kathy L Newell / Airi Tarutani / Shigeo Murayama / Masayuki Miyazaki / Yuko Saito / Mari Yoshida / Kazuko Hasegawa / Tammaryn Lashley / Tamas Revesz / Gabor G Kovacs / John van Swieten / Masaki Takao / Masato Hasegawa / Bernardino Ghetti / Maria Grazia Spillantini / Benjamin Ryskeldi-Falcon / Alexey G Murzin / Michel Goedert / Sjors H W Scheres / ![]() ![]() ![]() ![]() ![]() ![]() Abstract: Many age-dependent neurodegenerative diseases, such as Alzheimer's and Parkinson's, are characterized by abundant inclusions of amyloid filaments. Filamentous inclusions of the proteins tau, amyloid- ...Many age-dependent neurodegenerative diseases, such as Alzheimer's and Parkinson's, are characterized by abundant inclusions of amyloid filaments. Filamentous inclusions of the proteins tau, amyloid-β, α-synuclein and transactive response DNA-binding protein (TARDBP; also known as TDP-43) are the most common. Here we used structure determination by cryogenic electron microscopy to show that residues 120-254 of the lysosomal type II transmembrane protein 106B (TMEM106B) also form amyloid filaments in human brains. We determined the structures of TMEM106B filaments from a number of brain regions of 22 individuals with abundant amyloid deposits, including those resulting from sporadic and inherited tauopathies, amyloid-β amyloidoses, synucleinopathies and TDP-43 proteinopathies, as well as from the frontal cortex of 3 individuals with normal neurology and no or only a few amyloid deposits. We observed three TMEM106B folds, with no clear relationships between folds and diseases. TMEM106B filaments correlated with the presence of a 29-kDa sarkosyl-insoluble fragment and globular cytoplasmic inclusions, as detected by an antibody specific to the carboxy-terminal region of TMEM106B. The identification of TMEM106B filaments in the brains of older, but not younger, individuals with normal neurology indicates that they form in an age-dependent manner. | ||||||
History |
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Structure visualization
Movie |
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 155.1 KB | Display | ![]() |
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PDB format | ![]() | 125.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 14176MC ![]() 7qvcC ![]() 7qwgC ![]() 7qwlC ![]() 7qwmC M: map data used to model this data C: citing same article ( |
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Similar structure data | |
EM raw data | ![]() Data size: 1.0 TB Data #1: Unaligned multi-frame movies [micrographs - multiframe]) |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | ![]() Mass: 31156.318 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() Has ligand of interest | Y | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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EM experiment | Aggregation state: FILAMENT / 3D reconstruction method: helical reconstruction |
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Sample preparation
Component | Name: TMEM106B![]() |
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Source (natural) | Organism: ![]() ![]() |
Buffer solution | pH: 7.4 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied![]() ![]() |
Vitrification![]() | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source![]() ![]() |
Electron lens | Mode: BRIGHT FIELD![]() |
Image recording | Electron dose: 40 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
Software | Name: UCSF ChimeraX / Version: 1.1/v9 / Classification: model building / URL: https://www.rbvi.ucsf.edu/chimerax/ / Os: macOS / Type: package | |||||||||||||||
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EM software |
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CTF correction![]() | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||||||||
Helical symmerty | Angular rotation/subunit: -0.41 ° / Axial rise/subunit: 4.78 Å / Axial symmetry: C2 | |||||||||||||||
3D reconstruction![]() | Resolution: 3.64 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 12057 / Symmetry type: HELICAL |