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Creating and Applying a Reference to Facilitate the Discussion and Classification of Proteins in a Diverse Group
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Structure, function and evolution of three-finger toxins: mini proteins with multiple targets.

R Manjunatha Kini1, Robin Doley

  • 1Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore 117543, Singapore. dbskinim@nus.edu.sg

Toxicon : Official Journal of the International Society on Toxinology
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PubMed
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Three-finger toxins in snake venom, despite a shared structure, display diverse functions by binding to various receptors. Evolution and mutations drive their complex structure-function relationships.

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Area of Science:

  • Biochemistry
  • Toxicology
  • Molecular Biology

Background:

  • Snake venoms contain complex mixtures of peptides and proteins.
  • Three-finger toxins (3FTx) are a superfamily of non-enzymatic proteins found in all snake families.
  • 3FTx share a common structure of three beta-stranded loops from a central core with four conserved disulfide bonds.

Purpose of the Study:

  • To review the structural and functional diversity of three-finger toxins.
  • To explore the complex structure-function relationships of 3FTx.
  • To discuss the evolutionary mechanisms shaping 3FTx.

Main Methods:

  • Literature review of studies on three-finger toxins.
  • Analysis of structural and functional data.
  • Examination of evolutionary pathways.

Main Results:

  • Despite a conserved scaffold, 3FTx exhibit diverse biological effects by binding to different receptors.
  • Functional sites are located on various molecular surface segments.
  • Segmental exchange and point mutations contribute to functional diversification.

Conclusions:

  • The structural and functional diversity of 3FTx is driven by evolutionary adaptations.
  • Understanding 3FTx structure-function relationships is crucial for toxin research.
  • 3FTx represent a fascinating model for studying protein evolution and diversification.