5VR1
Structure of a Turripeptide from Unedogemmula bisaya venom
Summary for 5VR1
| Entry DOI | 10.2210/pdb5vr1/pdb |
| NMR Information | BMRB: 30291 |
| Descriptor | Turripeptide (1 entity in total) |
| Functional Keywords | unknown function |
| Biological source | Unedogemmula bisaya |
| Total number of polymer chains | 1 |
| Total formula weight | 1807.17 |
| Authors | Daly, N.L.,Imperial, J.S. (deposition date: 2017-05-09, release date: 2017-11-15, Last modification date: 2023-06-14) |
| Primary citation | 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 Cited by 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: 29090914DOI: 10.1021/acs.biochem.7b00485 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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