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7LYM

South African (B.1.351) SARS-CoV-2 spike protein variant (S-GSAS-B.1.351) in the RBD-down conformation

Summary for 7LYM
Entry DOI10.2210/pdb7lym/pdb
EMDB information23595
DescriptorSpike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
Functional Keywordssars-cov-2 spike protein trimer, viral protein
Biological sourceSevere acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2)
Total number of polymer chains3
Total formula weight434276.27
Authors
Gobeil, S.,Acharya, P. (deposition date: 2021-03-07, release date: 2021-03-31, Last modification date: 2021-08-18)
Primary citationGobeil, S.M.,Janowska, K.,McDowell, S.,Mansouri, K.,Parks, R.,Stalls, V.,Kopp, M.F.,Manne, K.,Li, D.,Wiehe, K.,Saunders, K.O.,Edwards, R.J.,Korber, B.,Haynes, B.F.,Henderson, R.,Acharya, P.
Effect of natural mutations of SARS-CoV-2 on spike structure, conformation, and antigenicity.
Science, 373:-, 2021
Cited by
PubMed Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants with multiple spike mutations enable increased transmission and antibody resistance. We combined cryo-electron microscopy (cryo-EM), binding, and computational analyses to study variant spikes, including one that was involved in transmission between minks and humans, and others that originated and spread in human populations. All variants showed increased angiotensin-converting enzyme 2 (ACE2) receptor binding and increased propensity for receptor binding domain (RBD)-up states. While adaptation to mink resulted in spike destabilization, the B.1.1.7 (UK) spike balanced stabilizing and destabilizing mutations. A local destabilizing effect of the RBD E484K mutation was implicated in resistance of the B.1.1.28/P.1 (Brazil) and B.1.351 (South Africa) variants to neutralizing antibodies. Our studies revealed allosteric effects of mutations and mechanistic differences that drive either interspecies transmission or escape from antibody neutralization.
PubMed: 34168071
DOI: 10.1126/science.abi6226
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.57 Å)
Structure validation

226707

数据于2024-10-30公开中

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