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-Structure paper
タイトル | Structures of SARS-CoV-2 spike protein alert noteworthy sites for the potential approaching variants. |
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ジャーナル・号・ページ | Virol Sin, Vol. 37, Issue 6, Page 938-941, Year 2022 |
掲載日 | 2022年11月8日 |
著者 | Xiaorui Xing / Lei Wang / Zhen Cui / Wangjun Fu / Tao Zheng / Lili Qin / Pingju Ge / Aidong Qian / Nan Wang / Shuai Yuan / |
PubMed 要旨 | • Deletion of residues 156–157 warps the neighboring beta-sheet and leads NTD and RBD to shift. • T859N stabilizes the packing of the 630 loop motif to make RBD standing transition more ...• Deletion of residues 156–157 warps the neighboring beta-sheet and leads NTD and RBD to shift. • T859N stabilizes the packing of the 630 loop motif to make RBD standing transition more difficult. • The overall structures of the closed state S complex from different variants resemble each other. • Mutations in FPPR may affect the overall structure of the trimeric spike protein. |
リンク | Virol Sin / PubMed:36368512 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.45 - 4.1 Å |
構造データ | EMDB-33721, PDB-7ybh: EMDB-33722, PDB-7ybi: EMDB-33723, PDB-7ybj: EMDB-33724, PDB-7ybk: EMDB-33725, PDB-7ybl: EMDB-33726, PDB-7ybm: EMDB-33727, PDB-7ybn: |
化合物 | ChemComp-NAG: |
由来 |
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キーワード | VIRAL PROTEIN / SARS-CoV-2 / Lambda / spike / Mu / B.1.620 |