1IMI
SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1
Summary for 1IMI
| Entry DOI | 10.2210/pdb1imi/pdb |
| Descriptor | PROTEIN (ALPHA-CONOTOXIN IMI) (1 entity in total) |
| Functional Keywords | neurotoxin, nicotinic acetylcholine receptor, postsynaptic, antagonist, acetylcholine receptor inhibitor |
| Biological source | Conus imperialis |
| Cellular location | Secreted: P50983 |
| Total number of polymer chains | 1 |
| Total formula weight | 1356.60 |
| Authors | Maslennikov, I.V.,Shenkarev, Z.O.,Zhmak, M.N.,Tsetlin, V.I.,Ivanov, V.T.,Arseniev, A.S. (deposition date: 1998-11-27, release date: 1999-04-23, Last modification date: 2024-10-30) |
| Primary citation | Maslennikov, I.V.,Shenkarev, Z.O.,Zhmak, M.N.,Ivanov, V.T.,Methfessel, C.,Tsetlin, V.I.,Arseniev, A.S. NMR spatial structure of alpha-conotoxin ImI reveals a common scaffold in snail and snake toxins recognizing neuronal nicotinic acetylcholine receptors. FEBS Lett., 444:275-280, 1999 Cited by PubMed Abstract: A 600 MHz NMR study of alpha-conotoxin ImI from Conus imperialis, targeting the alpha7 neuronal nicotinic acetylcholine receptor (nAChR), is presented. ImI backbone spatial structure is well defined basing on the NOEs, spin-spin coupling constants, and amide protons hydrogen-deuterium exchange data: rmsd of the backbone atom coordinates at the 2-12 region is 0.28 A in the 20 best structures. The structure is described as a type I beta-turn (positions 2-5) followed by a distorted helix (positions 5-11). Similar structural patterns can be found in all neuronal-specific alpha-conotoxins. Highly mobile side chains of the Asp-5, Arg-7 and Trp-10 residues form a single site for ImI binding to the alpha7 receptor. When depicted with opposite directions of the polypeptide chains, the ImI helix and the tip of the central loop of long chain snake neurotoxins demonstrate a common scaffold and similar positioning of the functional side chains, both of these structural elements appearing essential for binding to the neuronal nAChRs. PubMed: 10050774DOI: 10.1016/S0014-5793(99)00069-1 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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