NMR and restrained molecular dynamics study of the three-dimensional solution structure of toxin FS2, a specific blocker of the L-type calcium channel, isolated from black mamba venom.

@article{Albrand1995NMRAR,
  title={NMR and restrained molecular dynamics study of the three-dimensional solution structure of toxin FS2, a specific blocker of the L-type calcium channel, isolated from black mamba venom.},
  author={J P Albrand and Martin Blackledge and F Pascaud and Michelle Hollecker and Didier Marion},
  journal={Biochemistry},
  year={1995},
  volume={34 17},
  pages={5923-37}
}
The three-dimensional solution structure of toxin FS2, a 60-residue polypeptide isolated from the venom of black mamba snake (Dendroaspis polylepis polylepis), has been determined by nuclear magnetic resonance spectroscopy. Using 600 NOE constraints and 55 dihedral angle constraints, a set of 20 structures obtained from distance-geometry calculations was further refined by molecular dynamics calculations using a combined simulated annealing-restrained MD protocol. The resulting 20 conformers… CONTINUE READING

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This difference could be one of the factors leading to the distinct pharmacological properties - L - type calcium channel blocker for FS2 and cholinesterase inhibitor for fasciculin -- observed for these two subgroups of the " angusticeps - type " toxins .
The overall resulting three - fingered structure is similar to those already observed in several postsynaptic neurotoxins , cardiotoxins , and fasciculins , which all share with toxin FS2 the same network of four disulfide bridges .
This orientation is similar to that of fasciculins and cardiotoxins but opposite to that of neurotoxins .
The overall resulting three - fingered structure is similar to those already observed in several postsynaptic neurotoxins , cardiotoxins , and fasciculins , which all share with toxin FS2 the same network of four disulfide bridges .
This orientation is similar to that of fasciculins and cardiotoxins but opposite to that of neurotoxins .
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