Comparison of the structural features of botulinum neurotoxin and NTNH, a non-toxic accessory protein of the progenitor complex. (26th June 2008)

• Record Type: Journal Article
• Authors: Krebs, Kristine M.; Lebeda, Frank J.
• Is Part Of: Botulinum journal. Volume 1:Number 1(2008)
• Page Start: 116
• Page End: 134
• Publication Date: 2008-06-26
• Subjects: chimera -- coiled coil -- hydrophobicity -- mosaic -- protein domains -- protein folds -- sequence alignment -- botulinum neurotoxins -- BoNT -- botulism -- bioinformatics -- non-toxic non-hemagglutinin -- NTNH protein -- amino acid sequences; Botulinum toxin -- Periodicals; Clostridium botulinum -- Periodicals; Drug development -- Periodicals; 615.9529364
• Languages: English
• ISSNs: 1754-7318

Abstract

The non-toxic, non-hemagglutinin (NTNH) protein occurs with the seven progenitor serotypes of the botulinum neurotoxins (BoNTs). Bioinformatic techniques predict that the N- and C-termini of NTNH have the same folds as the corresponding domains of BoNT. In contrast, the sequence pattern for zinc-binding in the catalytic domain of BoNT is absent in NTNH. The intermediate domain of NTNH is predicted to have neither the coiled-coil nor the hydrophobic characteristics of the corresponding region of BoNT. BoNT and NTNH are hypothesised to have diverged in their amino acid sequences from a common ancestor which accounts for their structural and functional differences. [Received 24 October 2007; Accepted 21 November 2007]