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2MUN

Solution structure of mu-SLPTX3-Ssm6a

Summary for 2MUN
Entry DOI10.2210/pdb2mun/pdb
NMR InformationBMRB: 25223
DescriptorMu-scoloptoxin-Ssm6a (1 entity in total)
Functional Keywordstoxin, mu-slptx-ssm6a, crustacean hyperglycemic hormone, ion channel inhibitor
Biological sourceScolopendra mutilans (Chinese red-headed centipede)
Cellular locationSecreted: P0DL36
Total number of polymer chains1
Total formula weight5333.00
Authors
Undheim, E.A.B.,King, G.F.,Mobli, M. (deposition date: 2014-09-13, release date: 2015-06-24, Last modification date: 2024-11-20)
Primary citationUndheim, E.A.,Grimm, L.L.,Low, C.F.,Morgenstern, D.,Herzig, V.,Zobel-Thropp, P.,Pineda, S.S.,Habib, R.,Dziemborowicz, S.,Fry, B.G.,Nicholson, G.M.,Binford, G.J.,Mobli, M.,King, G.F.
Weaponization of a Hormone: Convergent Recruitment of Hyperglycemic Hormone into the Venom of Arthropod Predators.
Structure, 23:1283-1292, 2015
Cited by
PubMed Abstract: 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 α 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.
PubMed: 26073605
DOI: 10.1016/j.str.2015.05.003
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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