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7S6I

SARS-CoV-2-6P-Mut2 S protein

Summary for 7S6I
Entry DOI10.2210/pdb7s6i/pdb
EMDB information24876
DescriptorSpike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
Functional Keywordscovid, sars, cov-2, viral glycoprotein, spike, stabilizing mutations, coronavirus, viral protein, viral protein-immune system complex, viral protein/immune system
Biological sourceSevere acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2)
Total number of polymer chains3
Total formula weight438254.72
Authors
Ozorowski, G.,Torres, J.L.,Ward, A.B. (deposition date: 2021-09-14, release date: 2022-05-11, Last modification date: 2024-10-16)
Primary citationTorres, J.L.,Ozorowski, G.,Andreano, E.,Liu, H.,Copps, J.,Piccini, G.,Donnici, L.,Conti, M.,Planchais, C.,Planas, D.,Manganaro, N.,Pantano, E.,Paciello, I.,Pileri, P.,Bruel, T.,Montomoli, E.,Mouquet, H.,Schwartz, O.,Sala, C.,De Francesco, R.,Wilson, I.A.,Rappuoli, R.,Ward, A.B.
Structural insights of a highly potent pan-neutralizing SARS-CoV-2 human monoclonal antibody.
Proc.Natl.Acad.Sci.USA, 119:e2120976119-e2120976119, 2022
Cited by
PubMed Abstract: As the coronavirus disease 2019 (COVID-19) pandemic continues, there is a strong need for highly potent monoclonal antibodies (mAbs) that are resistant against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants of concern (VoCs). Here, we evaluate the potency of the previously described mAb J08 against these variants using cell-based assays and delve into the molecular details of the binding interaction using cryoelectron microscopy (cryo-EM) and X-ray crystallography. We show that mAb J08 has low nanomolar affinity against most VoCs and binds high on the receptor binding domain (RBD) ridge, away from many VoC mutations. These findings further validate the phase II/III human clinical trial underway using mAb J08 as a monoclonal therapy.
PubMed: 35549549
DOI: 10.1073/pnas.2120976119
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.2 Å)
Structure validation

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