Structural highlights
Publication Abstract from PubMed
We 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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ariki NK, Munoz LE, Armitage EL, Goodstein FR, George KG, Smith VL, Vetter I, Herzig V, King GF, Loening NM. Characterization of Three Venom Peptides from the Spitting Spider Scytodes thoracica. PLoS One. 2016 May 26;11(5):e0156291. doi: 10.1371/journal.pone.0156291., eCollection 2016. PMID:27227898 doi:http://dx.doi.org/10.1371/journal.pone.0156291
