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TitleStructural mechanisms behind the neutralisation of long-chain alpha-neurotoxins by broadly neutralising V H Hs discovered using a consensus antigen.
Journal, issue, pagesCommun Chem, Vol. 8, Page 209-209, Year 2025
Publish dateAug 2, 2024 (structure data deposition date)
AuthorsDamsbo, A. / Burlet, N.J. / Fernandez-Quintero, M.L. / Benard-Valle, M. / Overath, M.D. / Guadarrama-Martinez, A. / Vlamynck, A. / Bisbo, I. / Villalobos, C. / Tulika, T. ...Damsbo, A. / Burlet, N.J. / Fernandez-Quintero, M.L. / Benard-Valle, M. / Overath, M.D. / Guadarrama-Martinez, A. / Vlamynck, A. / Bisbo, I. / Villalobos, C. / Tulika, T. / Alagon, A. / Loeffler, J.R. / Ward, A.B. / Boddum, K. / Morth, J.P. / Rivera-de-Torre, E. / Laustsen, A.H.
External linksCommun Chem / PubMed:40681851
MethodsX-ray diffraction
Resolution3 Å
Structure data

PDB-9gcn:
Co-crystal VHH (TPL1158_01_C09) - alpha-cobratoxin (Naja kaouthia)
Method: X-RAY DIFFRACTION / Resolution: 3 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • vicugna pacos (alpaca)
  • naja kaouthia (monocled cobra)
KeywordsTOXIN / nanobody / VHH / atibody / antitoxin / snake toxin / antivenom / neutralising / neutralizing

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