A cross-over inhibitor of the botulinum neurotoxin light chain B: a natural product implicating an exosite mechanism of action
- PMID: 21203627
- PMCID: PMC3065946
- DOI: 10.1039/c0cc04078a
A cross-over inhibitor of the botulinum neurotoxin light chain B: a natural product implicating an exosite mechanism of action
Abstract
Clostridium botulinum produces the most lethal toxins known to man, as such they are high risk terrorist threats, and alarmingly there is no approved therapeutic. We report the first cross-over small molecule inhibitor of these neurotoxins and propose a mechanism by which it may impart its inhibitory activity.
Figures
Similar articles
-
Structure of botulinum neurotoxin type D light chain at 1.65 A resolution: repercussions for VAMP-2 substrate specificity.Biochemistry. 2006 Mar 14;45(10):3255-62. doi: 10.1021/bi052518r. Biochemistry. 2006. PMID: 16519520
-
Quaternary structure of botulinum and tetanus neurotoxins as probed by chemical cross-linking and native gel electrophoresis.Toxicon. 1994 Sep;32(9):1095-104. doi: 10.1016/0041-0101(94)90393-x. Toxicon. 1994. PMID: 7801345
-
The C terminus of the catalytic domain of type A botulinum neurotoxin may facilitate product release from the active site.J Biol Chem. 2013 Aug 16;288(33):24223-33. doi: 10.1074/jbc.M113.451286. Epub 2013 Jun 18. J Biol Chem. 2013. PMID: 23779108 Free PMC article.
-
Gaining ground: assays for therapeutics against botulinum neurotoxin.Trends Microbiol. 2010 Apr;18(4):164-72. doi: 10.1016/j.tim.2010.02.001. Epub 2010 Mar 4. Trends Microbiol. 2010. PMID: 20202845 Review.
-
Botulinum versus tetanus neurotoxins: why is botulinum neurotoxin but not tetanus neurotoxin a food poison?Toxicon. 1995 Dec;33(12):1541-7. doi: 10.1016/0041-0101(95)00094-1. Toxicon. 1995. PMID: 8866611 Review.
References
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources