1C4E の概要
| エントリーDOI | 10.2210/pdb1c4e/pdb |
| 関連するPDBエントリー | 2GUR |
| 分子名称 | PROTEIN (GURMARIN) (1 entity in total) |
| 機能のキーワード | gurmarin, sweet taste suppression, cystine knot, sweet taste transduction, plant protein |
| 由来する生物種 | Gymnema sylvestre |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 4220.95 |
| 構造登録者 | |
| 主引用文献 | Fletcher, J.I.,Dingley, A.J.,Smith, R.,Connor, M.,Christie, M.J.,King, G.F. High-resolution solution structure of gurmarin, a sweet-taste-suppressing plant polypeptide. Eur.J.Biochem., 264:525-533, 1999 Cited by PubMed Abstract: Gurmarin is a 35-residue polypeptide from the Asclepiad vine Gymnema sylvestre. It has been utilised as a pharmacological tool in the study of sweet-taste transduction because of its ability to selectively inhibit the neural response to sweet tastants in rats. We have chemically synthesised and folded gurmarin and determined its three-dimensional solution structure to high resolution using two-dimensional NMR spectroscopy. Structure calculations utilised 612 interproton-distance, 19 dihedral-angle, and 18 hydrogen-bond restraints. The structure is well defined for residues 3-34, with backbone and heavy atom rms differences of 0.27 +/- 0.09 A and 0.73 +/- 0.09 A, respectively. Gurmarin adopts a compact structure containing an antiparallel beta-hairpin (residues 22-34), several well-defined beta-turns, and a cystine-knot motif commonly observed in toxic and inhibitory polypeptides. Despite striking structural homology with delta-atracotoxin, a spider neurotoxin known to slow the inactivation of voltage-gated Na+ channels, we show that gurmarin has no effect on a variety of voltage-sensitive channels. PubMed: 10491100DOI: 10.1046/j.1432-1327.1999.00659.x 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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