1f31: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
Clostridium botulinum neurotoxins are among the most potent toxins to | 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 Structure== | ==About this Structure== | ||
| Line 26: | Line 26: | ||
[[Category: zinc]] | [[Category: zinc]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:17 2008'' | ||
Revision as of 10:34, 21 February 2008
|
CRYSTAL STRUCTURE OF CLOSTRIDIUM BOTULINUM NEUROTOXIN B COMPLEXED WITH A TRISACCHARIDE
Overview
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 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 Known structural/functional Site: ZN1. Full crystallographic information is available from OCA.
Reference
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 Thu Feb 21 12:34:17 2008
