3N7J
Crystal structure of botulinum neurotoxin serotype D binding domain
Summary for 3N7J
| Entry DOI | 10.2210/pdb3n7j/pdb |
| Related | 3N7K 3N7L 3N7M |
| Descriptor | Botulinum neurotoxin type D (2 entities in total) |
| Functional Keywords | botulinum neurotoxin, hcr/d, ganglioside binding loop, toxin |
| Biological source | Clostridium botulinum |
| Cellular location | Botulinum neurotoxin D light chain: Secreted. Botulinum neurotoxin D heavy chain: Secreted: P19321 |
| Total number of polymer chains | 1 |
| Total formula weight | 48237.25 |
| Authors | Fu, Z.,Baldwin, M.R.,Karalewitz, A.,Kroken, A.,Barbieri, J.T.,Kim, J.-J.P. (deposition date: 2010-05-27, release date: 2010-09-08, Last modification date: 2023-09-06) |
| Primary citation | Karalewitz, A.P.,Kroken, A.R.,Fu, Z.,Baldwin, M.R.,Kim, J.J.,Barbieri, J.T. Identification of a Unique Ganglioside Binding Loop within Botulinum Neurotoxins C and D-SA . Biochemistry, 49:8117-8126, 2010 Cited by PubMed Abstract: The botulinum neurotoxins (BoNTs) are the most potent protein toxins for humans. There are seven serotypes of BoNTs (A-G) based on a lack of cross antiserum neutralization. BoNTs utilize gangliosides as components of the host receptors for binding and entry into neurons. Members of BoNT/C and BoNT/D serotypes include mosaic toxins that are organized in D/C and C/D toxins. One D/C mosaic toxin, BoNT/D-South Africa (BoNT/D-SA), was not fully neutralized by immunization with BoNT serotype C or D, which stimulated this study. Here the crystal structures of the receptor binding domains of BoNT/C, BoNT/D, and BoNT/D-SA are presented. Biochemical and cell binding studies show that BoNT/C and BoNT/D-SA possess unique mechanisms for ganglioside binding. These studies provide new information about how the BoNTs can enter host cells as well as a basis for understanding the immunological diversity of these neurotoxins. PubMed: 20731382DOI: 10.1021/bi100865f PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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