Related Experiment Video
Updated: May 7, 2026

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
Published on: January 11, 2017
Evolution of three-finger toxins - a versatile mini protein scaffold
Abstract:
Among snake venom toxins, three-finger toxins - a superfamily of nonenzymatic proteins - are found in the venoms of all families of snakes. They share a common structure of three β-stranded loops extending from a central core containing all four conserved disulfide bonds. Despite the similar structural fold, they exhibit a wide variety of biological effects. This review describes briefly the structure-function relationships and evolution of this group of toxins. The functional sites in these šsibling' toxins are located on various segments of the molecular surface. This group of mini proteins appears to evolve through a combination of accelerated rate of exchange of segments as well as point mutations in exons.
Related Concept Videos
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Protein Folding
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Mechanical Protein Function
