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データを開く
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基本情報
| 登録情報 | ![]() | |||||||||
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| タイトル | High-resolution map of tau filament from progressive supranuclear palsy (PSP) case 1 | |||||||||
マップデータ | High-resolution map of tau filament from progressive supranuclear palsy (PSP) case 1. | |||||||||
試料 |
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キーワード | Tau protein / Amyloid fibril / PROTEIN FIBRIL | |||||||||
| 機能・相同性 | 機能・相同性情報plus-end-directed organelle transport along microtubule / histone-dependent DNA binding / negative regulation of establishment of protein localization to mitochondrion / neurofibrillary tangle / microtubule lateral binding / axonal transport / tubulin complex / positive regulation of protein localization to synapse / negative regulation of tubulin deacetylation / phosphatidylinositol bisphosphate binding ...plus-end-directed organelle transport along microtubule / histone-dependent DNA binding / negative regulation of establishment of protein localization to mitochondrion / neurofibrillary tangle / microtubule lateral binding / axonal transport / tubulin complex / positive regulation of protein localization to synapse / negative regulation of tubulin deacetylation / phosphatidylinositol bisphosphate binding / generation of neurons / rRNA metabolic process / axonal transport of mitochondrion / regulation of mitochondrial fission / axon development / regulation of chromosome organization / central nervous system neuron development / intracellular distribution of mitochondria / minor groove of adenine-thymine-rich DNA binding / lipoprotein particle binding / microtubule polymerization / negative regulation of mitochondrial membrane potential / dynactin binding / regulation of microtubule polymerization / apolipoprotein binding / main axon / protein polymerization / axolemma / glial cell projection / Caspase-mediated cleavage of cytoskeletal proteins / regulation of microtubule polymerization or depolymerization / negative regulation of mitochondrial fission / neurofibrillary tangle assembly / positive regulation of axon extension / regulation of cellular response to heat / Activation of AMPK downstream of NMDARs / synapse assembly / positive regulation of superoxide anion generation / regulation of long-term synaptic depression / positive regulation of protein localization / supramolecular fiber organization / cellular response to brain-derived neurotrophic factor stimulus / regulation of calcium-mediated signaling / cytoplasmic microtubule organization / positive regulation of microtubule polymerization / somatodendritic compartment / axon cytoplasm / astrocyte activation / stress granule assembly / phosphatidylinositol binding / nuclear periphery / regulation of microtubule cytoskeleton organization / protein phosphatase 2A binding / cellular response to reactive oxygen species / Hsp90 protein binding / microglial cell activation / cellular response to nerve growth factor stimulus / synapse organization / protein homooligomerization / PKR-mediated signaling / regulation of synaptic plasticity / SH3 domain binding / response to lead ion / microtubule cytoskeleton organization / memory / cytoplasmic ribonucleoprotein granule / neuron projection development / cell-cell signaling / single-stranded DNA binding / protein-folding chaperone binding / cellular response to heat / actin binding / microtubule cytoskeleton / cell body / growth cone / double-stranded DNA binding / protein-macromolecule adaptor activity / microtubule binding / dendritic spine / sequence-specific DNA binding / amyloid fibril formation / microtubule / learning or memory / neuron projection / regulation of autophagy / membrane raft / axon / negative regulation of gene expression / neuronal cell body / dendrite / DNA damage response / protein kinase binding / enzyme binding / mitochondrion / DNA binding / RNA binding / extracellular region / identical protein binding / nucleus / plasma membrane 類似検索 - 分子機能 | |||||||||
| 生物種 | Homo sapiens (ヒト) | |||||||||
| 手法 | らせん対称体再構成法 / クライオ電子顕微鏡法 / 解像度: 4.2 Å | |||||||||
データ登録者 | FItzpatrick AWP / Stowell MHB | |||||||||
| 資金援助 | 米国, 1件
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引用 | ジャーナル: Cell / 年: 2022タイトル: Homotypic fibrillization of TMEM106B across diverse neurodegenerative diseases. 著者: Andrew Chang / Xinyu Xiang / Jing Wang / Carolyn Lee / Tamta Arakhamia / Marija Simjanoska / Chi Wang / Yari Carlomagno / Guoan Zhang / Shikhar Dhingra / Manon Thierry / Jolien Perneel / Bavo ...著者: Andrew Chang / Xinyu Xiang / Jing Wang / Carolyn Lee / Tamta Arakhamia / Marija Simjanoska / Chi Wang / Yari Carlomagno / Guoan Zhang / Shikhar Dhingra / Manon Thierry / Jolien Perneel / Bavo Heeman / Lauren M Forgrave / Michael DeTure / Mari L DeMarco / Casey N Cook / Rosa Rademakers / Dennis W Dickson / Leonard Petrucelli / Michael H B Stowell / Ian R A Mackenzie / Anthony W P Fitzpatrick / ![]() 要旨: Misfolding and aggregation of disease-specific proteins, resulting in the formation of filamentous cellular inclusions, is a hallmark of neurodegenerative disease with characteristic filament ...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. | |||||||||
| 履歴 |
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構造の表示
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ダウンロードとリンク
-EMDBアーカイブ
| マップデータ | emd_26268.map.gz | 13.7 MB | EMDBマップデータ形式 | |
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| ヘッダ (付随情報) | emd-26268-v30.xml emd-26268.xml | 13.6 KB 13.6 KB | 表示 表示 | EMDBヘッダ |
| 画像 | emd_26268.png | 142 KB | ||
| Filedesc metadata | emd-26268.cif.gz | 5.6 KB | ||
| アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-26268 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-26268 | HTTPS FTP |
-検証レポート
| 文書・要旨 | emd_26268_validation.pdf.gz | 380.1 KB | 表示 | EMDB検証レポート |
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| 文書・詳細版 | emd_26268_full_validation.pdf.gz | 379.7 KB | 表示 | |
| XML形式データ | emd_26268_validation.xml.gz | 6.8 KB | 表示 | |
| CIF形式データ | emd_26268_validation.cif.gz | 7.8 KB | 表示 | |
| アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-26268 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-26268 | HTTPS FTP |
-関連構造データ
| 関連構造データ | ![]() 7u0zMC ![]() 7u10C ![]() 7u11C ![]() 7u12C ![]() 7u13C ![]() 7u14C ![]() 7u15C ![]() 7u16C ![]() 7u17C ![]() 7u18C C: 同じ文献を引用 ( M: このマップから作成された原子モデル |
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| 類似構造データ | 類似検索 - 機能・相同性 F&H 検索 |
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リンク
| EMDBのページ | EMDB (EBI/PDBe) / EMDataResource |
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| 「今月の分子」の関連する項目 |
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マップ
| ファイル | ダウンロード / ファイル: emd_26268.map.gz / 形式: CCP4 / 大きさ: 149.9 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| 注釈 | High-resolution map of tau filament from progressive supranuclear palsy (PSP) case 1. | ||||||||||||||||||||||||||||||||||||
| 投影像・断面図 | 画像のコントロール
画像は Spider により作成 | ||||||||||||||||||||||||||||||||||||
| ボクセルのサイズ | X=Y=Z: 1.1478 Å | ||||||||||||||||||||||||||||||||||||
| 密度 |
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| 対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||
| 詳細 | EMDB XML:
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-添付データ
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試料の構成要素
-全体 : TMEM106B(120-254) singlet amyloid fibril from dementia with Lewy ...
| 全体 | 名称: TMEM106B(120-254) singlet amyloid fibril from dementia with Lewy bodies (DLB) |
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| 要素 |
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-超分子 #1: TMEM106B(120-254) singlet amyloid fibril from dementia with Lewy ...
| 超分子 | 名称: TMEM106B(120-254) singlet amyloid fibril from dementia with Lewy bodies (DLB) タイプ: complex / ID: 1 / 親要素: 0 / 含まれる分子: all |
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| 由来(天然) | 生物種: Homo sapiens (ヒト) |
-分子 #1: Isoform Tau-E of Microtubule-associated protein tau
| 分子 | 名称: Isoform Tau-E of Microtubule-associated protein tau / タイプ: protein_or_peptide / ID: 1 / コピー数: 3 / 光学異性体: LEVO |
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| 由来(天然) | 生物種: Homo sapiens (ヒト) |
| 分子量 | 理論値: 11.836581 KDa |
| 組換発現 | 生物種: Homo sapiens (ヒト) |
| 配列 | 文字列: GGKVQIINKK LDLSNVQSKC GSKDNIKHVP GGGSVQIVYK PVDLSKVTSK CGSLGNIHHK PGGGQVEVKS EKLDFKDRVQ SKIGSLDNI THVPGGGNKK IETHKLTFRE N UniProtKB: Microtubule-associated protein tau |
-実験情報
-構造解析
| 手法 | クライオ電子顕微鏡法 |
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解析 | らせん対称体再構成法 |
| 試料の集合状態 | filament |
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試料調製
| 緩衝液 | pH: 7.4 |
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| 凍結 | 凍結剤: ETHANE |
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電子顕微鏡法
| 顕微鏡 | FEI TITAN KRIOS |
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| 撮影 | フィルム・検出器のモデル: GATAN K3 BIOQUANTUM (6k x 4k) 平均電子線量: 60.0 e/Å2 |
| 電子線 | 加速電圧: 300 kV / 電子線源: FIELD EMISSION GUN |
| 電子光学系 | 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD 最大 デフォーカス(公称値): 2.8000000000000003 µm 最小 デフォーカス(公称値): 1.4000000000000001 µm |
| 実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
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画像解析
| 最終 再構成 | 想定した対称性 - らせんパラメータ - Δz: 4.78 Å 想定した対称性 - らせんパラメータ - ΔΦ: -0.86 ° 想定した対称性 - らせんパラメータ - 軸対称性: C1 (非対称) 解像度のタイプ: BY AUTHOR / 解像度: 4.2 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 使用した粒子像数: 38000 |
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| CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION |
| 初期モデル | モデルのタイプ: NONE |
| 最終 角度割当 | タイプ: NOT APPLICABLE |
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コントローラー
万見について




キーワード
Homo sapiens (ヒト)
データ登録者
米国, 1件
引用







































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FIELD EMISSION GUN
