Crystal structure of a catalytically active, non-toxic endopeptidase derivative of Clostridium botulinum toxin A

Reference:

Masuyer, G., Thiyagarajan, N., James, P. L., Marks, P. M. H., Chaddock, J. A. and Acharya, K. R., 2009. Crystal structure of a catalytically active, non-toxic endopeptidase derivative of Clostridium botulinum toxin A. Biochemical and Biophysical Research Communications, 381 (1), pp. 50-53.

Related documents:

Official URL:

http://dx.doi.org/10.1016/j.bbrc.2009.02.003

Abstract

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 He domain is essential for BoNTs to bind the neuronal cell membrane, therefore, removal of the He 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.

Export

Actions (login required)