+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 8ys2 | ||||||||||||
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タイトル | Overall structure of Eastern Equine Encephalitis virus VLP in complex with the receptor VLDLR LA1-2 | ||||||||||||
要素 |
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キーワード | VIRUS LIKE PARTICLE / Eastern Equine Encephalitis virus / EEEV / receptor / complex / VLDLR / glycoprotein / VIRAL PROTEIN | ||||||||||||
機能・相同性 | 機能・相同性情報 reelin receptor activity / VLDL clearance / glycoprotein transport / ventral spinal cord development / very-low-density lipoprotein particle receptor activity / Reelin signalling pathway / very-low-density lipoprotein particle binding / low-density lipoprotein particle receptor activity / very-low-density lipoprotein particle clearance / reelin-mediated signaling pathway ...reelin receptor activity / VLDL clearance / glycoprotein transport / ventral spinal cord development / very-low-density lipoprotein particle receptor activity / Reelin signalling pathway / very-low-density lipoprotein particle binding / low-density lipoprotein particle receptor activity / very-low-density lipoprotein particle clearance / reelin-mediated signaling pathway / togavirin / very-low-density lipoprotein particle / positive regulation of dendrite development / T=4 icosahedral viral capsid / cargo receptor activity / dendrite morphogenesis / lipid transport / apolipoprotein binding / clathrin-coated pit / cholesterol metabolic process / VLDLR internalisation and degradation / receptor-mediated endocytosis / memory / symbiont-mediated suppression of host gene expression / calcium-dependent protein binding / nervous system development / symbiont-mediated suppression of host toll-like receptor signaling pathway / host cell cytoplasm / receptor complex / symbiont entry into host cell / lysosomal membrane / serine-type endopeptidase activity / fusion of virus membrane with host endosome membrane / calcium ion binding / host cell nucleus / virion attachment to host cell / host cell plasma membrane / structural molecule activity / virion membrane / signal transduction / proteolysis / RNA binding / membrane / plasma membrane 類似検索 - 分子機能 | ||||||||||||
生物種 | Eastern equine encephalitis virus (東部ウマ脳炎ウイルス) Homo sapiens (ヒト) | ||||||||||||
手法 | 電子顕微鏡法 / 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 5.2 Å | ||||||||||||
データ登録者 | Cao, D. / Ma, B. / Cao, Z. / Xu, X. / Zhang, X. / Xiang, Y. | ||||||||||||
資金援助 | 中国, 3件
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引用 | ジャーナル: Nat Commun / 年: 2024 タイトル: The receptor VLDLR binds Eastern Equine Encephalitis virus through multiple distinct modes. 著者: Duanfang Cao / Bingting Ma / Ziyi Cao / Xiaoyu Xu / Xinzheng Zhang / Ye Xiang / 要旨: Eastern Equine Encephalitis virus (EEEV) is an alphavirus that can cause severe diseases in infected humans. The very low-density lipoprotein receptor (VLDLR) was recently identified as a receptor of ...Eastern Equine Encephalitis virus (EEEV) is an alphavirus that can cause severe diseases in infected humans. The very low-density lipoprotein receptor (VLDLR) was recently identified as a receptor of EEEV. Herein, we performed cryo-electron microscopy structural and biochemistry studies on the specific interactions between EEEV and VLDLR. Our results show that VLDLR binds EEEV at three different sites A, B and C through its membrane-distal LDLR class A (LA) repeats. Site A is located in the cleft in between the E1-E2 heterodimers. Site B is located near the connecting β ribbon of E2 and is in proximity to site A, while site C is on the domain B of E2. The binding of VLDLR LAs to EEEV is in complex modes, including the LA1-2 and LA3-5 mediated two major modes. Disruption of the LA1-2 mediated binding significantly affect the cell attachment of EEEV. However, the mutation W132G of VLDLR impairs the binding of LA3, drives the switch of the binding modes, and significantly enhances the attachment of EEEV to the cell. The W132G variant of VLDLR could be identified in human genome and SNP sequences, implying that people with similar mutations in VLDLR may be highly susceptible to EEEV infection. | ||||||||||||
履歴 |
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-構造の表示
構造ビューア | 分子: MolmilJmol/JSmol |
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-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 8ys2.cif.gz | 837.1 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb8ys2.ent.gz | 表示 | PDB形式 | |
PDBx/mmJSON形式 | 8ys2.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
その他 | その他のダウンロード |
-検証レポート
文書・要旨 | 8ys2_validation.pdf.gz | 1.7 MB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 8ys2_full_validation.pdf.gz | 1.7 MB | 表示 | |
XML形式データ | 8ys2_validation.xml.gz | 121.9 KB | 表示 | |
CIF形式データ | 8ys2_validation.cif.gz | 182.7 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/ys/8ys2 ftp://data.pdbj.org/pub/pdb/validation_reports/ys/8ys2 | HTTPS FTP |
-関連構造データ
-リンク
-集合体
登録構造単位 |
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-要素
#1: タンパク質 | 分子量: 47984.246 Da / 分子数: 4 / 由来タイプ: 組換発現 由来: (組換発現) Eastern equine encephalitis virus (東部ウマ脳炎ウイルス) 発現宿主: Homo sapiens (ヒト) / 参照: UniProt: Q4QXJ7 #2: タンパク質 | 分子量: 47047.020 Da / 分子数: 4 / 由来タイプ: 組換発現 由来: (組換発現) Eastern equine encephalitis virus (東部ウマ脳炎ウイルス) 発現宿主: Homo sapiens (ヒト) / 参照: UniProt: Q4QXJ7 #3: タンパク質 | 分子量: 29178.846 Da / 分子数: 4 / Mutation: K67N / 由来タイプ: 組換発現 / 詳細: AAU95735.1 由来: (組換発現) Eastern equine encephalitis virus (東部ウマ脳炎ウイルス) 発現宿主: Homo sapiens (ヒト) / 参照: UniProt: Q4QXJ7, togavirin #4: タンパク質 | 分子量: 8854.691 Da / 分子数: 4 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: VLDLR / 発現宿主: Homo sapiens (ヒト) / 参照: UniProt: P98155 #5: 化合物 | ChemComp-CA / 研究の焦点であるリガンドがあるか | N | Has protein modification | Y | |
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-実験情報
-実験
実験 | 手法: 電子顕微鏡法 |
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EM実験 | 試料の集合状態: PARTICLE / 3次元再構成法: 単粒子再構成法 |
-試料調製
構成要素 | 名称: Eastern equine encephalitis virus / タイプ: VIRUS 詳細: EEEV Virus like particle in complexed with its receptor VLDLR LA1-2 Entity ID: #1-#4 / 由来: RECOMBINANT |
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由来(天然) | 生物種: Eastern equine encephalitis virus (東部ウマ脳炎ウイルス) |
由来(組換発現) | 生物種: Homo sapiens (ヒト) |
ウイルスについての詳細 | 中空か: YES / エンベロープを持つか: YES / 単離: OTHER / タイプ: VIRUS-LIKE PARTICLE |
天然宿主 | 生物種: Eastern equine encephalitis virus |
緩衝液 | pH: 8 |
試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
急速凍結 | 凍結剤: ETHANE |
-電子顕微鏡撮影
実験機器 | モデル: Titan Krios / 画像提供: FEI Company |
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顕微鏡 | モデル: FEI TITAN KRIOS |
電子銃 | 電子線源: FIELD EMISSION GUN / 加速電圧: 300 kV / 照射モード: FLOOD BEAM |
電子レンズ | モード: BRIGHT FIELD / 最大 デフォーカス(公称値): 1700 nm / 最小 デフォーカス(公称値): 1200 nm |
撮影 | 電子線照射量: 50 e/Å2 フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) |
-解析
CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
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3次元再構成 | 解像度: 5.2 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 15654 / 対称性のタイプ: POINT | ||||||||||||||||||||||||
拘束条件 |
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