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9II9

Crystal structure of SARS-CoV-2 neutralizing antibody K4-66

Summary for 9II9
Entry DOI10.2210/pdb9ii9/pdb
Descriptorantigen-binding fragments (Fabs) (2 entities in total)
Functional Keywordsantigen-binding fragments (fabs), immune system
Biological sourceHomo sapiens
More
Total number of polymer chains4
Total formula weight93043.53
Authors
Kimura, T.K.,Hashiguchi, T. (deposition date: 2024-06-19, release date: 2024-11-06, Last modification date: 2024-11-13)
Primary citationKuwata, T.,Kaku, Y.,Biswas, S.,Matsumoto, K.,Shimizu, M.,Kawanami, Y.,Uraki, R.,Okazaki, K.,Minami, R.,Nagasaki, Y.,Nagashima, M.,Yoshida, I.,Sadamasu, K.,Yoshimura, K.,Ito, M.,Kiso, M.,Yamayoshi, S.,Imai, M.,Ikeda, T.,Sato, K.,Toyoda, M.,Ueno, T.,Inoue, T.,Tanaka, Y.,Kimura, K.T.,Hashiguchi, T.,Sugita, Y.,Noda, T.,Morioka, H.,Kawaoka, Y.,Matsushita, S.
Induction of IGHV3-53 public antibodies with broadly neutralising activity against SARS-CoV-2 including Omicron subvariants in a Delta breakthrough infection case.
Ebiomedicine, 110:105439-105439, 2024
Cited by
PubMed Abstract: Emergence of SARS-CoV-2 variants that escape neutralising antibodies hampers the development of vaccines and therapeutic antibodies against SARS-CoV-2. IGHV3-53/3-66-derived public antibodies, which are generally specific to the prototype virus and are frequently induced in infected or vaccinated individuals, show minimal affinity maturation and high potency against prototype SARS-CoV-2.
PubMed: 39488016
DOI: 10.1016/j.ebiom.2024.105439
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.9 Å)
Structure validation

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