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TitleStructures of SARS-CoV-2 spike protein alert noteworthy sites for the potential approaching variants.
Journal, issue, pagesVirol Sin, Vol. 37, Issue 6, Page 938-941, Year 2022
Publish dateNov 8, 2022
AuthorsXiaorui Xing / Lei Wang / Zhen Cui / Wangjun Fu / Tao Zheng / Lili Qin / Pingju Ge / Aidong Qian / Nan Wang / Shuai Yuan /
PubMed Abstract• 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.
External linksVirol Sin / PubMed:36368512 / PubMed Central
MethodsEM (single particle)
Resolution3.45 - 3.9 Å
Structure data

33721

7ybh

EMDB-33721, PDB-7ybh:
SARS-CoV-2 lambda variant spike
Method: EM (single particle) / Resolution: 3.5 Å

33724

7ybk

EMDB-33724, PDB-7ybk:
SARS-CoV-2 B.1.620 variant spike (open state)
Method: EM (single particle) / Resolution: 3.9 Å

33725

7ybl

EMDB-33725, PDB-7ybl:
SARS-CoV-2 B.1.620 variant spike (close state)
Method: EM (single particle) / Resolution: 3.6 Å

33726

7ybm

EMDB-33726, PDB-7ybm:
SARS-CoV-2 C.1.2 variant spike (Close state)
Method: EM (single particle) / Resolution: 3.45 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • severe acute respiratory syndrome coronavirus 2
KeywordsVIRAL PROTEIN / SARS-CoV-2 / Lambda / spike / B.1.620

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