Structures of SARS-CoV-2 spike protein alert noteworthy sites for the potential approaching variants

• 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. • M...

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Autores principales: Xing, Xiaorui, Wang, Lei, Cui, Zhen, Fu, Wangjun, Zheng, Tao, Qin, Lili, Ge, Pingju, Qian, Aidong, Wang, Nan, Yuan, Shuai
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Wuhan Institute of Virology, Chinese Academy of Sciences 2022
Materias:
Letter
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9642027/
https://www.ncbi.nlm.nih.gov/pubmed/36368512
http://dx.doi.org/10.1016/j.virs.2022.11.003
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author Xing, Xiaorui
Wang, Lei
Cui, Zhen
Fu, Wangjun
Zheng, Tao
Qin, Lili
Ge, Pingju
Qian, Aidong
Wang, Nan
Yuan, Shuai
author_facet Xing, Xiaorui
Wang, Lei
Cui, Zhen
Fu, Wangjun
Zheng, Tao
Qin, Lili
Ge, Pingju
Qian, Aidong
Wang, Nan
Yuan, Shuai
author_sort Xing, Xiaorui
collection PubMed
description • 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.
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spelling pubmed-96420272022-11-14 Structures of SARS-CoV-2 spike protein alert noteworthy sites for the potential approaching variants Xing, Xiaorui Wang, Lei Cui, Zhen Fu, Wangjun Zheng, Tao Qin, Lili Ge, Pingju Qian, Aidong Wang, Nan Yuan, Shuai Virol Sin Letter • 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. Wuhan Institute of Virology, Chinese Academy of Sciences 2022-11-08 /pmc/articles/PMC9642027/ /pubmed/36368512 http://dx.doi.org/10.1016/j.virs.2022.11.003 Text en © 2022 The Authors https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Letter
Xing, Xiaorui
Wang, Lei
Cui, Zhen
Fu, Wangjun
Zheng, Tao
Qin, Lili
Ge, Pingju
Qian, Aidong
Wang, Nan
Yuan, Shuai
Structures of SARS-CoV-2 spike protein alert noteworthy sites for the potential approaching variants
title Structures of SARS-CoV-2 spike protein alert noteworthy sites for the potential approaching variants
title_full Structures of SARS-CoV-2 spike protein alert noteworthy sites for the potential approaching variants
title_fullStr Structures of SARS-CoV-2 spike protein alert noteworthy sites for the potential approaching variants
title_full_unstemmed Structures of SARS-CoV-2 spike protein alert noteworthy sites for the potential approaching variants
title_short Structures of SARS-CoV-2 spike protein alert noteworthy sites for the potential approaching variants
title_sort structures of sars-cov-2 spike protein alert noteworthy sites for the potential approaching variants
topic Letter
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9642027/
https://www.ncbi.nlm.nih.gov/pubmed/36368512
http://dx.doi.org/10.1016/j.virs.2022.11.003
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