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- W2998988007 abstract "Botulinum neurotoxins (BoNTs) are one of the most toxic proteins known to humans. Their molecular structure is comprised of three essential domains—a cell binding domain (H C ), translocation domain and catalytic domain (light chain) . The H C domain facilitates the highly specific binding of BoNTs to the neuronal membrane via a dual‐receptor complex involving a protein receptor and a ganglioside. Variation in activity/toxicity across subtypes of serotype A has been attributed to changes in protein and ganglioside interactions, and their implications are important in the design of novel BoNT‐based therapeutics. Here, we present the structure of BoNT/A3 cell binding domain (H C /A3) in complex with the ganglioside GD1a at 1.75 Å resolution. The structure revealed that six residues interact with the three outermost monosaccharides of GD1a through several key hydrogen bonding interactions. A detailed comparison of structures of H C /A3 with H C /A1 revealed subtle conformational differences at the ganglioside binding site upon carbohydrate binding." @default.
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- W2998988007 date "2020-01-28" @default.
- W2998988007 modified "2023-09-27" @default.
- W2998988007 title "Crystal structure of botulinum neurotoxin subtype A3 cell binding domain in complex with GD1a co‐receptor ganglioside" @default.
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- W2998988007 doi "https://doi.org/10.1002/2211-5463.12790" @default.
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