2MUN: Solution structure of mu-SLPTX3-Ssm6a

Arthropod venoms consist primarily of peptide toxins that are injected into their prey with devastating consequences. Venom proteins are thought to be recruited from endogenous body proteins and mutated to yield neofunctionalized toxins with remarkable affinity for specific subtypes of ion channels and receptors. However, the evolutionary history of venom peptides remains poorly understood. Here we show that a neuropeptide hormone has been convergently recruited into the venom of spiders and centipedes and evolved into a highly stable toxin through divergent modification of the ancestral gene. High-resolution structures of representative hormone-derived toxins revealed they possess a unique structure and disulfide framework and that the key structural adaptation in weaponization of the ancestral hormone was loss of a C-terminal alpha helix, an adaptation that occurred independently in spiders and centipedes. Our results raise a new paradigm for toxin evolution and highlight the value of structural information in providing insight into protein evolution.
PDB ID: 2MUNDownload
MMDB ID: 130232
PDB Deposition Date: 2014/9/13
Updated in MMDB: 2015/08
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 2MUN: monomeric; determined by author
Molecular Components in 2MUN
Label Count Molecule
Protein (1 molecule)
Molecule annotation
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Citing MMDB