Publication Abstract from PubMed
Botulinum neurotoxins (BoNTs) modulate cholinergic nerve terminals to result in neurotransmitter blockade. BoNTs consists of catalytic (LC), translocation (Hn) and cell-binding domains (Hc). The binding function of the Hc domain is essential for BoNTs to bind the neuronal cell membrane, therefore, removal of the Hc domain results in a product that retains the endopeptidase activity of the LC but is non-toxic. Thus, a molecule consisting of LC and Hn domains of BoNTs, termed LHn, is a suitable molecule for engineering novel therapeutics. The structure of LHA at 2.6 A reported here provides an understanding of the structural implications and challenges of engineering therapeutic molecules that combine functional properties of LHn of BoNTs with specific ligand partners to target different cell types.
Crystal structure of a catalytically active, non-toxic endopeptidase derivative of Clostridium botulinum toxin A.,Masuyer G, Thiyagarajan N, James PL, Marks PM, Chaddock JA, Acharya KR Biochem Biophys Res Commun. 2009 Mar 27;381(1):50-3. Epub 2009 Feb 8. PMID:19351593[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
