1AV3
POTASSIUM CHANNEL BLOCKER KAPPA CONOTOXIN PVIIA FROM C. PURPURASCENS, NMR, 20 STRUCTURES
Summary for 1AV3
Entry DOI | 10.2210/pdb1av3/pdb |
Descriptor | Kappa-conotoxin PVIIA (1 entity in total) |
Functional Keywords | kappa-conotoxin, potassium channel blocker, cystine knot |
Biological source | Conus purpurascens (Purple cone) |
Total number of polymer chains | 1 |
Total formula weight | 3282.87 |
Authors | Scanlon, M.J.,Naranjo, D.,Thomas, L.,Alewood, P.F.,Lewis, R.J.,Craik, D.J. (deposition date: 1997-09-24, release date: 1998-10-14, Last modification date: 2020-12-16) |
Primary citation | Scanlon, M.J.,Naranjo, D.,Thomas, L.,Alewood, P.F.,Lewis, R.J.,Craik, D.J. Solution structure and proposed binding mechanism of a novel potassium channel toxin kappa-conotoxin PVIIA. Structure, 5:1585-1597, 1997 Cited by PubMed Abstract: kappa-PVIIA is a 27-residue polypeptide isolated from the venom of Conus purpurascens and is the first member of a new class of conotoxins that block potassium channels. By comparison to other ion channels of eukaryotic cell membranes, voltage-sensitive potassium channels are relatively simple and methodology has been developed for mapping their interactions with small-peptide toxins. PVIIA, therefore, is a valuable new probe of potassium channel structure. This study of the solution structure and mode of channel binding of PVIIA forms the basis for mapping the interacting residues at the conotoxin-ion channel interface. PubMed: 9438859DOI: 10.1016/S0969-2126(97)00307-9 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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