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-Structure paper
タイトル | Distinct conformational states of SARS-CoV-2 spike protein. |
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ジャーナル・号・ページ | Science, Vol. 369, Issue 6511, Page 1586-1592, Year 2020 |
掲載日 | 2020年9月25日 |
著者 | Yongfei Cai / Jun Zhang / Tianshu Xiao / Hanqin Peng / Sarah M Sterling / Richard M Walsh / Shaun Rawson / Sophia Rits-Volloch / Bing Chen / |
PubMed 要旨 | Intervention strategies are urgently needed to control the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic. The trimeric viral spike (S) protein catalyzes fusion between viral ...Intervention strategies are urgently needed to control the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic. The trimeric viral spike (S) protein catalyzes fusion between viral and target cell membranes to initiate infection. Here, we report two cryo-electron microscopy structures derived from a preparation of the full-length S protein, representing its prefusion (2.9-angstrom resolution) and postfusion (3.0-angstrom resolution) conformations, respectively. The spontaneous transition to the postfusion state is independent of target cells. The prefusion trimer has three receptor-binding domains clamped down by a segment adjacent to the fusion peptide. The postfusion structure is strategically decorated by N-linked glycans, suggesting possible protective roles against host immune responses and harsh external conditions. These findings advance our understanding of SARS-CoV-2 entry and may guide the development of vaccines and therapeutics. |
リンク | Science / PubMed:32694201 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.9 - 3.0 Å |
構造データ | EMDB-22292, PDB-6xr8: EMDB-22293, PDB-6xra: |
化合物 | ChemComp-NAG: ChemComp-MAN: |
由来 |
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キーワード | VIRAL PROTEIN |