6thy

Botulinum neurotoxin A3 Hc domain in complex with GD1a

spinqualitylabelsall models 6thy, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6thy is a 1 chain structure with sequence from Clostridium botulinum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.75Å Ligands: ACT, BGC, EDO, GAL, NGA, P6G, PEG, SIA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q3LRX9_CLOBO Publication Abstract from PubMed 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 (HC ), translocation domain (HN ), and catalytic domain (LC). The HC 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 (HC /A3) in complex with the ganglioside GD1a at 1.75 A 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 HC /A3 with HC /A1 revealed subtle conformational differences at the ganglioside binding site (GBS) upon carbohydrate binding. Crystal structure of botulinum neurotoxin subtype A3 cell binding domain in complex with GD1a co-receptor ganglioside.,Gregory KS, Liu SM, Acharya KR FEBS Open Bio. 2020 Jan 16. doi: 10.1002/2211-5463.12790. PMID:31945264 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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