6OVJ
NMR structure of truncated alpha conotoxin SII: Ile-SII(3-14)
Summary for 6OVJ
| Entry DOI | 10.2210/pdb6ovj/pdb |
| Related | 6OTB |
| Descriptor | Alpha-conotoxin S2 (1 entity in total) |
| Functional Keywords | toxin |
| Biological source | Conus striatus (Striated cone) |
| Total number of polymer chains | 1 |
| Total formula weight | 1314.54 |
| Authors | Chin, Y.K.-Y.,Wilhelm, P.,Alewood, P.F. (deposition date: 2019-05-08, release date: 2020-05-06, Last modification date: 2024-11-20) |
| Primary citation | Wilhelm, P.,Luna-Ramirez, K.,Chin, Y.K.,Dekan, Z.,Abraham, N.,Tae, H.S.,Chow, C.Y.,Eagles, D.A.,King, G.F.,Lewis, R.J.,Adams, D.J.,Alewood, P.F. Cysteine-Rich alpha-Conotoxin SII Displays Novel Interactions at the Muscle Nicotinic Acetylcholine Receptor. Acs Chem Neurosci, 13:1245-1250, 2022 Cited by PubMed Abstract: α-Conotoxins that target muscle nicotinic acetylcholine receptors (nAChRs) commonly fall into two structural classes, frameworks I and II containing two and three disulfide bonds, respectively. Conotoxin SII is the sole member of the cysteine-rich framework II with ill-defined interactions at the nAChRs. Following directed synthesis of α-SII, NMR analysis revealed a well-defined structure containing a 3-helix frequently employed by framework I α-conotoxins; α-SII acted at the muscle nAChR with half-maximal inhibitory concentrations (IC) of 120 nM (adult) and 370 nM (fetal) though weakly at neuronal nAChRs. Truncation of α-SII to a two disulfide bond amidated peptide with framework I disulfide connectivity led to similar activity. Surprisingly, the more constrained α-SII was less stable under mild reducing conditions and displayed a unique docking mode at the nAChR. PubMed: 35357806DOI: 10.1021/acschemneuro.1c00857 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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