Abstract
Background: The mechanism of botulinum neurotoxin D light chain (LC/D) substrate recognition is not well defined. Results: A dual recognition strategy employed by LC/D was revealed, in which one site of VAMP-2 was recognized by two independent, functionally similar LC/D sites that were complementary to each other. Conclusion: LC/D utilizes a unique mechanism for substrate recognition. Significance: This study provides insights for LC/D engineering and antitoxin development. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
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CITATION STYLE
Guo, J., & Chen, S. (2013). Unique substrate recognition mechanism of the botulinum neurotoxin D light chain. Journal of Biological Chemistry, 288(39), 27881–27887. https://doi.org/10.1074/jbc.M113.491134
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