EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Evolution of the SARS-CoV-2 spike protein in the human host.
ジャーナル・号・ページ	Nat Commun, Vol. 13, Issue 1, Page 1178, Year 2022
掲載日	2022年3月4日
著者	Antoni G Wrobel / Donald J Benton / Chloë Roustan / Annabel Borg / Saira Hussain / Stephen R Martin / Peter B Rosenthal / John J Skehel / Steven J Gamblin /
PubMed 要旨	Recently emerged variants of SARS-CoV-2 contain in their surface spike glycoproteins multiple substitutions associated with increased transmission and resistance to neutralising antibodies. We have ...Recently emerged variants of SARS-CoV-2 contain in their surface spike glycoproteins multiple substitutions associated with increased transmission and resistance to neutralising antibodies. We have examined the structure and receptor binding properties of spike proteins from the B.1.1.7 (Alpha) and B.1.351 (Beta) variants to better understand the evolution of the virus in humans. Spikes of both variants have the same mutation, N501Y, in the receptor-binding domains. This substitution confers tighter ACE2 binding, dependent on the common earlier substitution, D614G. Each variant spike has acquired other key changes in structure that likely impact virus pathogenesis. The spike from the Alpha variant is more stable against disruption upon binding ACE2 receptor than all other spikes studied. This feature is linked to the acquisition of a more basic substitution at the S1-S2 furin site (also observed for the variants of concern Delta, Kappa, and Omicron) which allows for near-complete cleavage. In the Beta variant spike, the presence of a new substitution, K417N (also observed in the Omicron variant), in combination with the D614G, stabilises a more open spike trimer, a conformation required for receptor binding. Our observations suggest ways these viruses have evolved to achieve greater transmissibility in humans.
リンク	Nat Commun / PubMed:35246509 / PubMed Central
手法	EM (単粒子)
解像度	2.8 - 4.1 Å
構造データ	14225 7r0z EMDB-14225, PDB-7r0z: Dissociated S1 domain of Alpha Variant SARS-CoV-2 Spike bound to ACE2 (Non-Uniform Refinement) 手法: EM (単粒子) / 解像度: 3.5 Å 14226 7r10 EMDB-14226, PDB-7r10: Dissociated S1 domain of Alpha Variant SARS-CoV-2 Spike bound to ACE2 手法: EM (単粒子) / 解像度: 4.0 Å 14227 7r11 EMDB-14227, PDB-7r11: Dissociated S1 domain of Beta Variant SARS-CoV-2 Spike bound to ACE2 (Non-Uniform Refinement) 手法: EM (単粒子) / 解像度: 3.5 Å 14228 7r12 EMDB-14228, PDB-7r12: Dissociated S1 domain of Mink Variant SARS-CoV-2 Spike bound to ACE2 (Non-Uniform Refinement) 手法: EM (単粒子) / 解像度: 3.3 Å 14229 7r13 EMDB-14229, PDB-7r13: Alpha Variant SARS-CoV-2 Spike in Closed conformation 手法: EM (単粒子) / 解像度: 3.6 Å 14230 7r14 EMDB-14230, PDB-7r14: Alpha Variant SARS-CoV-2 Spike with 1 Erect RBD 手法: EM (単粒子) / 解像度: 3.4 Å 14231 7r15 EMDB-14231, PDB-7r15: Alpha Variant SARS-CoV-2 Spike with 2 Erect RBDs 手法: EM (単粒子) / 解像度: 4.1 Å 14232 7r16 EMDB-14232, PDB-7r16: Beta Variant SARS-CoV-2 Spike with 1 Erect RBD 手法: EM (単粒子) / 解像度: 3.5 Å 14233 7r17 EMDB-14233, PDB-7r17: Beta Variant SARS-CoV-2 Spike with 2 Erect RBDs 手法: EM (単粒子) / 解像度: 3.7 Å 14234 7r18 EMDB-14234, PDB-7r18: Mink Variant SARS-CoV-2 Spike in Closed conformation 手法: EM (単粒子) / 解像度: 3.0 Å 14235 7r19 EMDB-14235, PDB-7r19: Mink Variant SARS-CoV-2 Spike with 2 Erect RBDs 手法: EM (単粒子) / 解像度: 3.3 Å 14236 7r1a EMDB-14236, PDB-7r1a: Furin Cleaved Alpha Variant SARS-CoV-2 Spike in complex with 3 ACE2 手法: EM (単粒子) / 解像度: 3.9 Å 14237 7r1b EMDB-14237, PDB-7r1b: Mink Variant SARS-CoV-2 Spike with 1 Erect RBD 手法: EM (単粒子) / 解像度: 2.8 Å
化合物	ChemComp-ZN: Unknown entry ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose / N-アセチル-β-D-グルコサミン / N-アセチルグルコサミン ChemComp-HOH: WATER / 水
由来	homo sapiens (ヒト) severe acute respiratory syndrome coronavirus 2 (SARSコロナウイルス2)
キーワード	VIRAL PROTEIN (ウイルスタンパク質) / Spike / SARS-CoV-2 (SARSコロナウイルス2)