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Journal Articles Archives de l'Institut Pasteur de Tunis Year : 2010

[Snake venom metalloproteinases: structure, biosynthesis and function(s)].

Les Métalloprotéases des venins de serpents: structure, biosynthèse et fonction(s)

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Abstract

The biochemical and the pharmacological characterization of snake venoms revealed an important structural and functional polymorphism of proteins which they contain. Among them, snake venom metalloproteases (SVMPs) constitute approximatively 20 to 60% of the whole venom proteins. During the last decades, a significant progress was performed against structure studies and the biosynthesis of the SVMPs. Indeed, several metalloproteases were isolated and characterized against their structural and pharmacological properties. In this review, we report the most important properties concerning the classification, the structure of the various domains of the SVMPs as well as their biosynthesis and their activities as potential therapeutic agents.
La caractéristique biochimique et pharmacologique des venins de serpents révèle un polymorphisme structural et fonctionnel de plus en plus important des protéines qu'ils contiennent. Parmi ces protéines, on retrouve les métalloprotéases des venins de serpents (SVPMs) qui contiennent environ 20 à 60% des protéines totales du venin. Durant les dernières décennies, un progrès significatif a été réalisé quant aux études de la structure et la biosynthèse des SVMPs. [...]
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Dates and versions

pasteur-00621020 , version 1 (09-09-2011)

Identifiers

  • HAL Id : pasteur-00621020 , version 1
  • PUBMED : 21604456

Cite

I. Limam, M. El Ayeb, N. Marrakchi. Les Métalloprotéases des venins de serpents: structure, biosynthèse et fonction(s). Archives de l'Institut Pasteur de Tunis, 2010, 87 (1-2), pp.3-15. ⟨pasteur-00621020⟩

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