7SBR
One RBD-up 2 of pre-fusion SARS-CoV-2 Kappa variant spike protein
Summary for 7SBR
Entry DOI | 10.2210/pdb7sbr/pdb |
EMDB information | 24986 |
Descriptor | Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
Functional Keywords | viral protein |
Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2) |
Total number of polymer chains | 3 |
Total formula weight | 456422.86 |
Authors | Zhang, J.,Xiao, T.S.,Cai, Y.F.,Peng, H.Q.,Volloch, S.R.,Chen, B. (deposition date: 2021-09-25, release date: 2021-11-03, Last modification date: 2024-10-23) |
Primary citation | Zhang, J.,Xiao, T.,Cai, Y.,Lavine, C.L.,Peng, H.,Zhu, H.,Anand, K.,Tong, P.,Gautam, A.,Mayer, M.L.,Walsh Jr., R.M.,Rits-Volloch, S.,Wesemann, D.R.,Yang, W.,Seaman, M.S.,Lu, J.,Chen, B. Membrane fusion and immune evasion by the spike protein of SARS-CoV-2 Delta variant. Science, 374:1353-1360, 2021 Cited by PubMed Abstract: The Delta variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has outcompeted previously prevalent variants and become a dominant strain worldwide. We report the structure, function, and antigenicity of its full-length spike (S) trimer as well as those of the Gamma and Kappa variants, and compare their characteristics with the G614, Alpha, and Beta variants. Delta S can fuse membranes more efficiently at low levels of cellular receptor angiotensin converting enzyme 2 (ACE2), and its pseudotyped viruses infect target cells substantially faster than the other five variants, possibly accounting for its heightened transmissibility. Each variant shows different rearrangement of the antigenic surface of the amino-terminal domain of the S protein but only makes produces changes in the receptor binding domain (RBD), making the RBD a better target for therapeutic antibodies. PubMed: 34698504DOI: 10.1126/science.abl9463 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.3 Å) |
Structure validation
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