9EH4
Solution structure of alpha conotoxin LvID
Summary for 9EH4
| Entry DOI | 10.2210/pdb9eh4/pdb |
| NMR Information | BMRB: 31219 |
| Descriptor | Alpha conotoxin LvID (1 entity in total) |
| Functional Keywords | conotoxin, toxin |
| Biological source | Conus lividus |
| Total number of polymer chains | 1 |
| Total formula weight | 1748.01 |
| Authors | Harvey, P.J.,Craik, D.J. (deposition date: 2024-11-22, release date: 2025-04-23, Last modification date: 2025-05-07) |
| Primary citation | Guo, M.,Zhu, X.,Ma, T.,Xu, C.,Zhangsun, D.,Yu, J.,Kaas, Q.,Harvey, P.J.,McIntosh, J.M.,Craik, D.J.,Luo, S. Selective Inhibition of Rat alpha 7 Nicotinic Acetylcholine Receptors by LvID, a Newly Characterized alpha 4/7-Conotoxin from Conus lividus . J.Med.Chem., 68:8163-8173, 2025 Cited by PubMed Abstract: The α7 nicotinic acetylcholine receptors (nAChRs), identified in peripheral and central nervous systems, are crucial for cognitive function, memory, inflammation, and are linked to disorders like Alzheimer's disease (AD), lung cancer, myasthenia gravis, and atherosclerosis. Here we report that a novel α4/7-conotoxin (CTx) LvID, from , potently inhibits rat α7 nAChRs expressed in oocytes with an IC of 13.8 nM, showing little activity against other rat nAChR subtypes. The structure of LvID was elucidated using nuclear magnetic resonance (NMR) spectroscopy and comprises a short helix braced by disulfide bonds. The key residues of LvID that bind to the α7 nAChRs were determined from a series of alanine mutants. Molecular simulation provided a possible explanation for the activity and specificity of LvID binding to α7 nAChRs. This finding offers a vital pharmacological tool for investigating the structural features and functional mechanisms of α7 nAChRs. PubMed: 40205658DOI: 10.1021/acs.jmedchem.4c02810 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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