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Structural comparison of three crystalline complexes of a peptidic toxin with a synaptic acetylcholine recognition protein.

Abstract : Many peptidic toxins from animal venoms target neuronal or peripheral synaptic receptors with high affinities and specificities. Hence, these toxins are not only potent natural weapons but also precise molecular tools for pharmacological studies of their receptors. Although they belong to various structural and/or functional subfamilies, they often share similar molecular features, such as a highly reticulated scaffold presenting specific binding determinants.
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https://hal.archives-ouvertes.fr/hal-00134316
Contributor : Corinne Dumonceaud Connect in order to contact the contributor
Submitted on : Thursday, March 1, 2007 - 3:15:10 PM
Last modification on : Friday, January 21, 2022 - 12:26:01 PM

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  • HAL Id : hal-00134316, version 1
  • PUBMED : 17192648

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yves Bourne, Scott B Hansen, Gerlind Sulzenbacher, Todd T Talley, Tom Huxford, et al.. Structural comparison of three crystalline complexes of a peptidic toxin with a synaptic acetylcholine recognition protein.. Journal of Molecular Neuroscience, Humana Press, 2006, 30 (1-2), pp.103-4. ⟨hal-00134316⟩

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