+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 7pvd | ||||||
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タイトル | Structure of the membrane soluble spike complex from the Lassa virus in a C1-symmetric map focused on the ectodomain | ||||||
要素 |
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キーワード | VIRAL PROTEIN / Spike complex / glycoprotein | ||||||
機能・相同性 | 機能・相同性情報 host cell Golgi membrane / receptor-mediated endocytosis of virus by host cell / host cell endoplasmic reticulum membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane / virion membrane / membrane / metal ion binding 類似検索 - 分子機能 | ||||||
生物種 | Lassa virus (ウイルス) | ||||||
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: 3.7 Å | ||||||
データ登録者 | Diskin, R. / Katz, M. | ||||||
資金援助 | 1件
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引用 | ジャーナル: Nature / 年: 2022 タイトル: Structure and receptor recognition by the Lassa virus spike complex. 著者: Michael Katz / Jonathan Weinstein / Maayan Eilon-Ashkenazy / Katrin Gehring / Hadas Cohen-Dvashi / Nadav Elad / Sarel J Fleishman / Ron Diskin / 要旨: Lassa virus (LASV) is a human pathogen, causing substantial morbidity and mortality. Similar to other Arenaviridae, it presents a class-I spike complex on its surface that facilitates cell entry. The ...Lassa virus (LASV) is a human pathogen, causing substantial morbidity and mortality. Similar to other Arenaviridae, it presents a class-I spike complex on its surface that facilitates cell entry. The virus's cellular receptor is matriglycan, a linear carbohydrate that is present on α-dystroglycan, but the molecular mechanism that LASV uses to recognize this glycan is unknown. In addition, LASV and other arenaviruses have a unique signal peptide that forms an integral and functionally important part of the mature spike; yet the structure, function and topology of the signal peptide in the membrane remain uncertain. Here we solve the structure of a complete native LASV spike complex, finding that the signal peptide crosses the membrane once and that its amino terminus is located in the extracellular region. Together with a double-sided domain-switching mechanism, the signal peptide helps to stabilize the spike complex in its native conformation. This structure reveals that the LASV spike complex is preloaded with matriglycan, suggesting the mechanism of binding and rationalizing receptor recognition by α-dystroglycan-tropic arenaviruses. This discovery further informs us about the mechanism of viral egress and may facilitate the rational design of novel therapeutics that exploit this binding site. | ||||||
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-構造の表示
ムービー |
ムービービューア |
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構造ビューア | 分子: MolmilJmol/JSmol |
-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 7pvd.cif.gz | 210.4 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb7pvd.ent.gz | 171.1 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 7pvd.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 | 7pvd_validation.pdf.gz | 1.7 MB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 7pvd_full_validation.pdf.gz | 1.7 MB | 表示 | |
XML形式データ | 7pvd_validation.xml.gz | 43.1 KB | 表示 | |
CIF形式データ | 7pvd_validation.cif.gz | 56.4 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/pv/7pvd ftp://data.pdbj.org/pub/pdb/validation_reports/pv/7pvd | HTTPS FTP |
-関連構造データ
-リンク
-集合体
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