5VR1

Structure of a Turripeptide from Unedogemmula bisaya venom

5VR1 の概要

• エントリーDOI: 10.2210/pdb5vr1/pdb
• NMR情報: BMRB: 30291
• 分子名称: Turripeptide (1 entity in total)
• 機能のキーワード: unknown function
• 由来する生物種: Unedogemmula bisaya
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1807.17

構造登録者

Daly, N.L.,Imperial, J.S. (登録日: 2017-05-09, 公開日: 2017-11-15, 最終更新日: 2023-06-14)

主引用文献

Omaga, C.A.,Carpio, L.D.,Imperial, J.S.,Daly, N.L.,Gajewiak, J.,Flores, M.S.,Espino, S.S.,Christensen, S.,Filchakova, O.M.,Lopez-Vera, E.,Raghuraman, S.,Olivera, B.M.,Concepcion, G.P.
Structure and Biological Activity of a Turripeptide from Unedogemmula bisaya Venom.
Biochemistry, 56:6051-6060, 2017

PubMed Abstract: The 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-NH (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: C-C C-C, C-C. The peptide inhibited the activity of the α9α10 nicotinic acetylcholine receptor with relatively low affinity (IC, 10.2 μM). Initial Constellation Pharmacology data revealed an excitatory activity of ubi3a on a specific subset of mouse dorsal root ganglion neurons.

PubMed: 29090914
DOI: 10.1021/acs.biochem.7b00485

実験手法

SOLUTION NMR