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TitleA Single-Domain Llama Antibody Potently Inhibits the Enzymatic Activity of Botulinum Neurotoxin by Binding to the Non-Catalytic alpha-Exosite Binding Region.
Journal, issue, pagesJ. Mol. Biol., Vol. 397, Page 1106-1118, Year 2010
Publish dateOct 4, 2009 (structure data deposition date)
AuthorsDong, J. / Thompson, A.A. / Fan, Y. / Lou, J. / Conrad, F. / Ho, M. / Pires-Alves, M. / Wilson, B.A. / Stevens, R.C. / Marks, J.D.
External linksJ. Mol. Biol. / PubMed:20138889
MethodsX-ray diffraction
Resolution2.6 Å
Structure data

PDB-3k3q:
Crystal Structure of a Llama Antibody complexed with the C. Botulinum Neurotoxin Serotype A Catalytic Domain
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • lama glama (llama)
  • clostridium botulinum a str. hall (bacteria)
KeywordsIMMUNE SYSTEM / llama / VHH / antibody / botulinum / neurotoxin / BoNT / Cell junction / Cell membrane / Cytoplasm / Disulfide bond / Hydrolase / Membrane / Metal-binding / Metalloprotease / Pharmaceutical / Protease / Secreted / Synapse / Toxin / Transmembrane / Zinc

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