1AG7
CONOTOXIN GS, NMR, 20 STRUCTURES
Summary for 1AG7
Entry DOI | 10.2210/pdb1ag7/pdb |
Descriptor | CONOTOXIN GS (1 entity in total) |
Functional Keywords | neurotoxin, mu-conotoxin, sodium channel blocker, cystine knot motif |
Biological source | Conus geographus (geography cone) |
Total number of polymer chains | 1 |
Total formula weight | 3630.15 |
Authors | Hill, J.M.,Alewood, P.F.,Craik, D.J. (deposition date: 1997-04-03, release date: 1998-04-08, Last modification date: 2022-02-16) |
Primary citation | Hill, J.M.,Alewood, P.F.,Craik, D.J. Solution structure of the sodium channel antagonist conotoxin GS: a new molecular caliper for probing sodium channel geometry. Structure, 5:571-583, 1997 Cited by PubMed Abstract: The venoms of Conus snails contain small, disulfide-rich inhibitors of voltage-dependent sodium channels. Conotoxin GS is a 34-residue polypeptide isolated from Conus geographus that interacts with the extracellular entrance of skeletal muscle sodium channels to prevent sodium ion conduction. Although conotoxin GS binds competitively with mu conotoxin GIIIA to the sodium channel surface, the two toxin types have little sequence identity with one another, and conotoxin GS has a four-loop structural framework rather than the characteristic three-loop mu-conotoxin framework. The structural study of conotoxin GS will form the basis for establishing a structure-activity relationship and understanding its interaction with the pore region of sodium channels. PubMed: 9115446DOI: 10.1016/S0969-2126(97)00212-8 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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