5vr1
From Proteopedia
Structure of a Turripeptide from Unedogemmula bisaya venom
Structural highlights
Publication Abstract from PubMedThe turripeptide ubi3a was isolated from the venom of the marine gastropod Unedogemmula bisaya, family Turridae, by bioassay-guided purification; both native and synthetic ubi3a elicited prolonged tremors when injected intracranially into mice. The sequence of the peptide, DCCOCOAGAVRCRFACC-NH2 (O = 4-hydroxyproline) follows the framework III pattern for cysteines (CC-C-C-CC) in the M-superfamily of conopeptides. The three-dimensional structure determined by NMR spectroscopy indicated a disulfide connectivity that is not found in conopeptides with the cysteine framework III: C1-C4, C2-C6, C3-C5. The peptide inhibited the activity of the alpha9alpha10 nicotinic acetylcholine receptor with relatively low affinity (IC50, 10.2 muM). Initial Constellation Pharmacology data revealed an excitatory activity of ubi3a on a specific subset of mouse dorsal root ganglion neurons. Structure and Biological Activity of a Turripeptide from Unedogemmula bisaya Venom.,Omaga CA, Carpio LD, Imperial JS, Daly NL, Gajewiak J, Flores MS, Espino SS, Christensen S, Filchakova OM, Lopez-Vera E, Raghuraman S, Olivera BM, Concepcion GP Biochemistry. 2017 Nov 14;56(45):6051-6060. doi: 10.1021/acs.biochem.7b00485., Epub 2017 Nov 1. PMID:29090914[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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