1XGC
ALPHA CONOTOXIN GI: 2-3;7-13 DISULFIDE BOND ISOMER, NMR, 25 STRUCTURES
1XGC の概要
エントリーDOI | 10.2210/pdb1xgc/pdb |
分子名称 | ALPHA-CONOTOXIN GI (1 entity in total) |
機能のキーワード | neurotoxin, alpha-conotoxin, nicotinic acetylcholine recepto disulfide bond isomers |
細胞内の位置 | Secreted: P01519 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 1442.65 |
構造登録者 | |
主引用文献 | Gehrmann, J.,Alewood, P.F.,Craik, D.J. Structure determination of the three disulfide bond isomers of alpha-conotoxin GI: a model for the role of disulfide bonds in structural stability. J.Mol.Biol., 278:401-415, 1998 Cited by PubMed Abstract: The three possible disulfide bonded isomers of alpha-conotoxin GI have been selectively synthesised and their structures determined by 1H NMR spectroscopy. alpha-Conotoxin GI derives from the venom of Conus geographus and is a useful neuropharmacological tool as it selectively binds to the nicotinic acetylcholine receptor (nAChR), a ligand-gated ion channel involved in nerve signal transmission. The peptide has the sequence ECCNPACGRHYSC-NH2, and the three disulfide bonded isomers are referred to as GI(2-7;3-13), GI(2-13;3-7) and GI(2-3;7-13). The NMR structure for the native isomer GI(2-7;3-13) is of excellent quality, with a backbone pairwise RMSD of 0.16 A for a family of 35 structures, and comprises primarily a distorted 310 helix between residues 5 to 11. The two non-native isomers exhibit multiple conformers in solution, with the major populated forms being different in structure both from each other and from the native form. Structure-activity relationships for the native GI(2-7;3-13) as well as the role of the disulfide bonds on folding and stability of the three isomers are examined. It is concluded that the disulfide bonds in alpha-conotoxin GI play a crucial part in determining both the structure and stability of the peptide. A trend for increased conformational heterogeneity was observed in the order of GI(2-7;3-13) DOI: 10.1006/jmbi.1998.1701 主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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