5fzw | pdb_00005fzw
High resolution solution NMR structure of the spider venom peptide U3- scytotoxin-Sth1h
Structural highlights
FunctionU31H_SCYTH Probable insect neurotoxin with ion channel impairing activity (Probable). Does not show activity on 45 human receptors from 9 families (5-hydroxytryptamine, adrenergic, dopamine, muscarinic, histamine, neurotransmitter, opioid, sigma, and gaba(A) receptors) (PubMed:27227898). In vivo, when mixed with U3-SYTX-Sth1a does not cause paralytic or lethal activity when injected into crickets (PubMed:27227898). It is noteworthy that crickets are evolutionarily distant from prey species (PubMed:27227898).[1] Publication Abstract from PubMedWe present the solution-state NMR structures and preliminary functional characterizations of three venom peptides identified from the spitting spider Scytodes thoracica. Despite little sequence identity to other venom peptides, structural characterization reveals that these peptides contain an inhibitor cystine knot motif common to many venom peptides. These are the first structures for any peptide or protein from spiders of the Scytodidae family. Many venom peptides target neuronal ion channels or receptors. However, we have not been able to determine the target of these Scytodes peptides so we can only state with certainty the channels and receptors that they do not target. Characterization of Three Venom Peptides from the Spitting Spider Scytodes thoracica.,Ariki NK, Munoz LE, Armitage EL, Goodstein FR, George KG, Smith VL, Vetter I, Herzig V, King GF, Loening NM PLoS One. 2016 May 26;11(5):e0156291. doi: 10.1371/journal.pone.0156291., eCollection 2016. PMID:27227898[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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