1f31

From Proteopedia
Revision as of 11:57, 30 October 2007 by OCA (talk | contribs)
Jump to navigation Jump to search
File:1f31.gif


1f31, resolution 2.6Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF CLOSTRIDIUM BOTULINUM NEUROTOXIN B COMPLEXED WITH A TRISACCHARIDE

OverviewOverview

Clostridium botulinum neurotoxins are among the most potent toxins to, humans. The crystal structures of intact C. botulinum neurotoxin type B, (BoNT/B) and its complex with sialyllactose, determined at 1. 8 and 2.6 A, resolution, respectively, provide insight into its catalytic and binding, sites. The position of the belt region in BoNT/B is different from that in, BoNT/A; this observation presents interesting possibilities for designing, specific inhibitors that could be used to block the activity of this, neurotoxin. The structures of BoNT/B and its complex with sialyllactose, provide a detailed description of the active site and a model for, interactions between the toxin and its cell surface receptor. The latter, may provide valuable information for recombinant vaccine development.

About this StructureAbout this Structure

1F31 is a [Single protein] structure of sequence from [Clostridium botulinum] with ZN and SO4 as [ligands]. Active as [Bontoxilysin], with EC number [3.4.24.69]. Structure known Active Site: ZN1. Full crystallographic information is available from [OCA].

ReferenceReference

Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B., Swaminathan S, Eswaramoorthy S, Nat Struct Biol. 2000 Aug;7(8):693-9. PMID:10932256

Page seeded by OCA on Tue Oct 30 11:02:14 2007

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA