Great stuff! If this greater diversity in 3FT structure is indeed accompanied with more diversified 3FT functions (perhaps mediated through 3FT interaction with currently uncharacterized receptors?), these toxins could prove to be productive hunting grounds for new pharmaceuticals.



It is interesting that so much structural and functional diversity exists within snake-venom toxin families. Another family of proteins that displays great diversity among its members is the immunoglobulin (antibody) family. Like many of the snake-toxin families, the immunoglobulins are a multi-gene family. And, like snake toxins, they evolved to interact with foreign organisms in a manner that is advantageous to their owners. Structural diversity in immunoglobulins allows them to effectively interact with just about any foreign, potentially disease-causing organisms like bacteria, viruses, and fungi. The mechanisms underlying this necessary diversity in antibody structure are varied, including things like gene duplication / diversification, gene rearrangement, terminal NT addition, and targeted mutagenesis / somatic hypermutation. These processes have made it so a finite number of immunoglobulin genes produce the seemingly infinite number of structurally distinct immunoglobulins needed to fend off environmental pathogens.



Wouldn’t it be interesting if mechanisms similar to those underlying antibody diversity were behind some of this snake-venom toxin diversity?



It really does boggle the mind!



Cheers,

WK

[ Show Entire Thread ]