Molecular moulds with multiple missions: functional sites in three-finger toxins

Clin Exp Pharmacol Physiol. 2002 Sep;29(9):815-22. doi: 10.1046/j.1440-1681.2002.03725.x.

Abstract

1. Snake venoms are complex mixtures of pharmacologically active peptides and proteins. 2. These protein toxins belong to a small number of superfamilies of proteins. The present review describes structure-function relationships of three-finger toxins. 3. All toxins share a common structure of three beta-stranded loops extending from a central core. However, they bind to different receptors/acceptors and exhibit a wide variety of biological effects. 4. Thus, the structure-function relationships of this group of toxins are complicated and challenging. 5. Studies have shown that the functional sites in these "sibling" toxins are located on various segments of the molecular surface.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Asia
  • Australia
  • Humans
  • Models, Molecular*
  • Neurotoxins / chemistry*
  • Neurotoxins / metabolism
  • Neurotoxins / pharmacology
  • Snake Venoms / chemistry*
  • Snake Venoms / metabolism
  • Snake Venoms / pharmacology
  • Structure-Activity Relationship

Substances

  • Neurotoxins
  • Snake Venoms