1IEO
SOLUTION STRUCTURE OF MRIB-NH2
Summary for 1IEO
| Entry DOI | 10.2210/pdb1ieo/pdb |
| Related | 1IEN |
| Descriptor | PROTEIN MRIB-NH2 (1 entity in total) |
| Functional Keywords | conotoxin, neuronal noradrenaline transporter, toxin |
| Cellular location | Secreted: P58810 |
| Total number of polymer chains | 1 |
| Total formula weight | 1397.73 |
| Authors | Sharpe, I.A.,Gehrmann, J.,Loughnan, M.L.,Thomas, L.,Adams, D.A.,Atkins, A.,Palant, E.,Craik, D.J.,Adams, D.J.,Alewood, P.F.,Lewis, R.J. (deposition date: 2001-04-10, release date: 2002-04-03, Last modification date: 2022-02-23) |
| Primary citation | Sharpe, I.A.,Gehrmann, J.,Loughnan, M.L.,Thomas, L.,Adams, D.A.,Atkins, A.,Palant, E.,Craik, D.J.,Adams, D.J.,Alewood, P.F.,Lewis, R.J. Two new classes of conopeptides inhibit the alpha1-adrenoceptor and noradrenaline transporter. Nat.Neurosci., 4:902-907, 2001 Cited by PubMed Abstract: Cone snails use venom containing a cocktail of peptides ('conopeptides') to capture their prey. Many of these peptides also target mammalian receptors, often with exquisite selectivity. Here we report the discovery of two new classes of conopeptides. One class targets alpha1-adrenoceptors (rho-TIA from the fish-hunting Conus tulipa), and the second class targets the neuronal noradrenaline transporter (chi-MrIA and chi-MrIB from the mollusk-hunting C. marmoreus). rho-TIA and chi-MrIA selectively modulate these important membrane-bound proteins. Both peptides act as reversible non-competitive inhibitors and provide alternative avenues for the identification of inhibitor drugs. PubMed: 11528421DOI: 10.1038/nn0901-902 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
