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Structural basis for functional diversity of animal toxins

Published online by Cambridge University Press:  05 December 2011

André Ménez
Affiliation:
Département d'Ingénierie et d'Etudes des Protéines, CE Saclay, 91190, Gif-sur-Yvette, France
François Bontems
Affiliation:
Département d'Ingénierie et d'Etudes des Protéines, CE Saclay, 91190, Gif-sur-Yvette, France
Christian Roumestand
Affiliation:
Département d'Ingénierie et d'Etudes des Protéines, CE Saclay, 91190, Gif-sur-Yvette, France
Bernard Gilquin
Affiliation:
Département d'Ingénierie et d'Etudes des Protéines, CE Saclay, 91190, Gif-sur-Yvette, France
Flavio Toma
Affiliation:
Département d'Ingénierie et d'Etudes des Protéines, CE Saclay, 91190, Gif-sur-Yvette, France
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Synopsis:

The diversity of biological functions that are exerted by toxins from snake and scorpion venoms is associated with a limited number of structural frameworks. At present, one predominant basic fold has been observed among scorpion toxins whereas six folds have been found among snake toxins. Most toxin folds have the capacity to accept multiple insertions, deletions and mutations and to exert various recognition functions. We suggest that such folds may serve as guides to engineer new protein functions.

Type
Research Article
Copyright
Copyright © Royal Society of Edinburgh 1992

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References

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