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Understanding how biotic interactions shape the genomes of the interacting species is a long-sought goal of evolutionary biology that has been hampered by the scarcity of tractable systems in which specific genomic features can be linked to complex phenotypes involved in interspecific interactions. In this review we present the compelling case of evolved resistance to the toxic challenge of venomous...
Scorpion venoms are complex mixtures of dozens or even hundreds of distinct proteins, many of which are inter-genome active elements. Fifty years after the first scorpion toxin sequences were determined, chromatography-assisted purification followed by automated protein sequencing or gene cloning, on a case-by-case basis, accumulated nearly 250 amino acid sequences of scorpion venom components. A...
Scorpion toxins classified as β-class are reviewed using a new paradigm. Four distinct sub types are recognized: “classical”, “Tsγ-like”, “excitatory” and “depressant” β-scorpion toxins. Recent experimental data have made possible to identify the interacting interfaces of the Na + channel-receptor site 4 with some of these toxins. The voltage-sensor trapping mechanism proposed for the action...
Scorpion venoms contain a large number of bioactive components. Several of the long-chain peptides were shown to be responsible for neurotoxic effects, due to their ability to recognize Na + channels and to cause impairment of channel functions. Here, we revisited the basic paradigms in the study of these peptides in the light of recent data concerning their structure–function relationships,...
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