Structural highlights
Function
Q9LBR1_CLOBO
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Identification of a Unique Ganglioside Binding Loop within Botulinum Neurotoxins C and D-SA .,Karalewitz AP, Kroken AR, Fu Z, Baldwin MR, Kim JJ, Barbieri JT Biochemistry. 2010 Aug 23. PMID:20731382[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Karalewitz AP, Kroken AR, Fu Z, Baldwin MR, Kim JJ, Barbieri JT. Identification of a Unique Ganglioside Binding Loop within Botulinum Neurotoxins C and D-SA . Biochemistry. 2010 Aug 23. PMID:20731382 doi:10.1021/bi100865f
