6CEI
Solution NMR Structure of Conotoxin GXIA from Conus geographus
Summary for 6CEI
| Entry DOI | 10.2210/pdb6cei/pdb |
| NMR Information | BMRB: 30406 |
| Descriptor | GXIA (1 entity in total) |
| Functional Keywords | conotoxin conus geographus disulfide-rich peptide inhibitor cystine knot, toxin |
| Biological source | Conus geographus (Geography cone) |
| Total number of polymer chains | 1 |
| Total formula weight | 3344.95 |
| Authors | Armstrong, D.A.,Rosengren, K.J. (deposition date: 2018-02-12, release date: 2018-03-07, Last modification date: 2024-11-20) |
| Primary citation | Armstrong, D.A.,Jin, A.H.,Braga Emidio, N.,Lewis, R.J.,Alewood, P.F.,Rosengren, K.J. Chemical Synthesis and NMR Solution Structure of Conotoxin GXIA from Conus geographus . Mar Drugs, 19:-, 2021 Cited by PubMed Abstract: Conotoxins are disulfide-rich peptides found in the venom of cone snails. Due to their exquisite potency and high selectivity for a wide range of voltage and ligand gated ion channels they are attractive drug leads in neuropharmacology. Recently, cone snails were found to have the capability to rapidly switch between venom types with different proteome profiles in response to predatory or defensive stimuli. A novel conotoxin, GXIA (original name G117), belonging to the I-subfamily was identified as the major component of the predatory venom of piscivorous . Using 2D solution NMR spectroscopy techniques, we resolved the 3D structure for GXIA, the first structure reported for the I-subfamily and framework XI family. The 32 amino acid peptide is comprised of eight cysteine residues with the resultant disulfide connectivity forming an ICK+1 motif. With a triple stranded β-sheet, the GXIA backbone shows striking similarity to several tarantula toxins targeting the voltage sensor of voltage gated potassium and sodium channels. Supported by an amphipathic surface, the structural evidence suggests that GXIA is able to embed in the membrane and bind to the voltage sensor domain of a putative ion channel target. PubMed: 33530397DOI: 10.3390/md19020060 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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