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7SBR

One RBD-up 2 of pre-fusion SARS-CoV-2 Kappa variant spike protein

Summary for 7SBR
Entry DOI10.2210/pdb7sbr/pdb
EMDB information24986
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-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
Functional Keywordsviral protein
Biological sourceSevere acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2)
Total number of polymer chains3
Total formula weight456422.86
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 citationZhang, 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: 34698504
DOI: 10.1126/science.abl9463
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.3 Å)
Structure validation

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