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データを開く
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基本情報
| 登録情報 | データベース: PDB / ID: 6x2a | |||||||||||||||
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| タイトル | SARS-CoV-2 u1S2q 1-RBD Up Spike Protein Trimer | |||||||||||||||
要素 | Spike glycoprotein | |||||||||||||||
キーワード | VIRAL PROTEIN / Trimer | |||||||||||||||
| 機能・相同性 | 機能・相同性情報symbiont-mediated disruption of host tissue / Maturation of spike protein / Translation of Structural Proteins / Virion Assembly and Release / host cell surface / host extracellular space / viral translation / symbiont-mediated-mediated suppression of host tetherin activity / Induction of Cell-Cell Fusion / structural constituent of virion ...symbiont-mediated disruption of host tissue / Maturation of spike protein / Translation of Structural Proteins / Virion Assembly and Release / host cell surface / host extracellular space / viral translation / symbiont-mediated-mediated suppression of host tetherin activity / Induction of Cell-Cell Fusion / structural constituent of virion / entry receptor-mediated virion attachment to host cell / membrane fusion / Attachment and Entry / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / positive regulation of viral entry into host cell / receptor-mediated virion attachment to host cell / host cell surface receptor binding / symbiont-mediated suppression of host innate immune response / receptor ligand activity / endocytosis involved in viral entry into host cell / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / symbiont entry into host cell / virion attachment to host cell / SARS-CoV-2 activates/modulates innate and adaptive immune responses / host cell plasma membrane / virion membrane / identical protein binding / membrane / plasma membrane 類似検索 - 分子機能 | |||||||||||||||
| 生物種 | ![]() | |||||||||||||||
| 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: 3.3 Å | |||||||||||||||
データ登録者 | Henderson, R. / Acharya, P. | |||||||||||||||
| 資金援助 | 米国, 4件
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引用 | ジャーナル: Nat Struct Mol Biol / 年: 2020タイトル: Controlling the SARS-CoV-2 spike glycoprotein conformation. 著者: Rory Henderson / Robert J Edwards / Katayoun Mansouri / Katarzyna Janowska / Victoria Stalls / Sophie M C Gobeil / Megan Kopp / Dapeng Li / Rob Parks / Allen L Hsu / Mario J Borgnia / Barton ...著者: Rory Henderson / Robert J Edwards / Katayoun Mansouri / Katarzyna Janowska / Victoria Stalls / Sophie M C Gobeil / Megan Kopp / Dapeng Li / Rob Parks / Allen L Hsu / Mario J Borgnia / Barton F Haynes / Priyamvada Acharya / ![]() 要旨: The coronavirus (CoV) spike (S) protein, involved in viral-host cell fusion, is the primary immunogenic target for virus neutralization and the current focus of many vaccine design efforts. The ...The coronavirus (CoV) spike (S) protein, involved in viral-host cell fusion, is the primary immunogenic target for virus neutralization and the current focus of many vaccine design efforts. The highly flexible S-protein, with its mobile domains, presents a moving target to the immune system. Here, to better understand S-protein mobility, we implemented a structure-based vector analysis of available β-CoV S-protein structures. Despite an overall similarity in domain organization, we found that S-proteins from different β-CoVs display distinct configurations. Based on this analysis, we developed two soluble ectodomain constructs for the SARS-CoV-2 S-protein, in which the highly immunogenic and mobile receptor binding domain (RBD) is either locked in the all-RBDs 'down' position or adopts 'up' state conformations more readily than the wild-type S-protein. These results demonstrate that the conformation of the S-protein can be controlled via rational design and can provide a framework for the development of engineered CoV S-proteins for vaccine applications. #1: ジャーナル: bioRxiv / 年: 2020 タイトル: Controlling the SARS-CoV-2 Spike Glycoprotein Conformation. 著者: Rory Henderson / Robert J Edwards / Katayoun Mansouri / Katarzyna Janowska / Victoria Stalls / Sophie Gobeil / Megan Kopp / Allen Hsu / Mario Borgnia / Rob Parks / Barton F Haynes / Priyamvada Acharya / ![]() 要旨: The coronavirus (CoV) viral host cell fusion spike (S) protein is the primary immunogenic target for virus neutralization and the current focus of many vaccine design efforts. The highly flexible S- ...The coronavirus (CoV) viral host cell fusion spike (S) protein is the primary immunogenic target for virus neutralization and the current focus of many vaccine design efforts. The highly flexible S-protein, with its mobile domains, presents a moving target to the immune system. Here, to better understand S-protein mobility, we implemented a structure-based vector analysis of available β-CoV S-protein structures. We found that despite overall similarity in domain organization, different β-CoV strains display distinct S-protein configurations. Based on this analysis, we developed two soluble ectodomain constructs in which the highly immunogenic and mobile receptor binding domain (RBD) is locked in either the all-RBDs 'down' position or is induced to display a previously unobserved in SARS-CoV-2 2-RBDs 'up' configuration. These results demonstrate that the conformation of the S-protein can be controlled via rational design and provide a framework for the development of engineered coronavirus spike proteins for vaccine applications. | |||||||||||||||
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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: Molmil Jmol/JSmol |
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ダウンロードとリンク
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ダウンロード
| PDBx/mmCIF形式 | 6x2a.cif.gz | 515.4 KB | 表示 | PDBx/mmCIF形式 |
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| PDB形式 | pdb6x2a.ent.gz | 398 KB | 表示 | PDB形式 |
| PDBx/mmJSON形式 | 6x2a.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 | 6x2a_validation.pdf.gz | 881.8 KB | 表示 | wwPDB検証レポート |
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| 文書・詳細版 | 6x2a_full_validation.pdf.gz | 891.9 KB | 表示 | |
| XML形式データ | 6x2a_validation.xml.gz | 68.9 KB | 表示 | |
| CIF形式データ | 6x2a_validation.cif.gz | 108.6 KB | 表示 | |
| アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/x2/6x2a ftp://data.pdbj.org/pub/pdb/validation_reports/x2/6x2a | HTTPS FTP |
-関連構造データ
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リンク
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集合体
| 登録構造単位 | ![]()
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要素
| #1: タンパク質 | 分子量: 140790.453 Da / 分子数: 3 / 断片: ectodomain (UNP residues 16-1208) / 変異: F855Y+N856I+A570L+T572I / 由来タイプ: 組換発現 由来: (組換発現) ![]() 遺伝子: S, 2 / 発現宿主: Homo sapiens (ヒト) / 参照: UniProt: P0DTC2Has 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 |
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試料調製
| 構成要素 | 名称: Severe acute respiratory syndrome coronavirus 2 / タイプ: VIRUS / Entity ID: all / 由来: RECOMBINANT |
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| 由来(天然) | 生物種: ![]() |
| 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: NO / エンベロープを持つか: YES / 単離: OTHER / タイプ: VIRION |
| 緩衝液 | pH: 7.4 |
| 試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
| 試料支持 | 詳細: unspecified |
| 急速凍結 | 凍結剤: ETHANE |
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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 |
| 撮影 | 電子線照射量: 66.82 e/Å2 / フィルム・検出器のモデル: GATAN K3 (6k x 4k) |
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解析
| CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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| 対称性 | 点対称性: C1 (非対称) |
| 3次元再構成 | 解像度: 3.3 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 255013 / 対称性のタイプ: POINT |
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コントローラー
万見について






米国, 4件
引用
UCSF Chimera
















PDBj




Homo sapiens (ヒト)
