7ce2

The Crystal structure of TeNT Hc complexed with neutralizing antibody

spinqualitylabelsall models 7ce2, resolution 2.01Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7ce2 is a 3 chain structure with sequence from Clostridium tetani and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.01Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Four potent native human monoclonal antibodies (mAbs) targeting distinct epitopes on tetanus toxin (TeNT) are isolated with neutralization potency ranging from approximately 17 mg to 6 mg each that are equivalent to 250 IU of human anti-TeNT immunoglobulin. TT0170 binds fragment B, and TT0069 and TT0155 bind fragment AB. mAb TT0067 binds fragment C and blocks the binding of TeNT to gangliosides. The co-crystal structure of TT0067 with fragment C of TeNT at a 2.0-A resolution demonstrates that mAb TT0067 directly occupies the W pocket of one of the receptor binding sites on TeNT, resulting in blocking the binding of TeNT to ganglioside on the surface of host cells. This study reveals at the atomic level the mechanism of action by the TeNT neutralizing antibody. The key neutralization epitope on the fragment C of TeNT identified in our work provides the critical information for the development of fragment C of TeNT as a better and safer tetanus vaccine. Structural basis of tetanus toxin neutralization by native human monoclonal antibodies.,Wang Y, Wu C, Yu J, Lin S, Liu T, Zan L, Li N, Hong P, Wang X, Jia Z, Li J, Wang Y, Zhang M, Yuan X, Li C, Xu W, Zheng W, Wang X, Liao HX Cell Rep. 2021 May 4;35(5):109070. doi: 10.1016/j.celrep.2021.109070. PMID:33951441 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Antibody 3D structures Monoclonal Antibodies 3D structures Tetanus toxin

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