1IDH

THE NMR SOLUTION STRUCTURE OF THE COMPLEX FORMED BETWEEN ALPHA-BUNGAROTOXIN AND AN 18MER COGNATE PEPTIDE

1IDH の概要

• エントリーDOI: 10.2210/pdb1idh/pdb
• 関連するPDBエントリー: 1IDG 1IDI 1IDL
• NMR情報: BMRB: 5025
• 分子名称: ALPHA-BUNGAROTOXIN, ACETYLCHOLINE RECEPTOR PROTEIN, ALPHA CHAIN (2 entities in total)
• 機能のキーワード: alpha-bungarotoxin, nicotinic acetylcholine receptor, alpha 1 subunit, protein-protein interaction, cation-pi interaction, toxin
• 由来する生物種: Torpedo californica (Pacific electric ray); 詳細
• 細胞内の位置: Secreted: P60615; Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein: P02710
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 10430.01

構造登録者

Zeng, H.,Moise, L.,Grant, M.A.,Hawrot, E. (登録日: 2001-04-04, 公開日: 2001-04-25, 最終更新日: 2022-02-23)

主引用文献

Zeng, H.,Moise, L.,Grant, M.A.,Hawrot, E.
The solution structure of the complex formed between alpha-bungarotoxin and an 18-mer cognate peptide derived from the alpha 1 subunit of the nicotinic acetylcholine receptor from Torpedo californica.
J.Biol.Chem., 276:22930-22940, 2001

PubMed Abstract: The region encompassing residues 181-98 on the alpha1 subunit of the muscle-type nicotinic acetylcholine receptor forms a major determinant for the binding of alpha-neurotoxins. We have prepared an (15)N-enriched 18-amino acid peptide corresponding to the sequence in this region to facilitate structural elucidation by multidimensional NMR. Our aim was to determine the structural basis for the high affinity, stoichiometric complex formed between this cognate peptide and alpha-bungarotoxin, a long alpha-neurotoxin. Resonances in the complex were assigned through heteronuclear and homonuclear NMR experiments, and the resulting interproton distance constraints were used to generate ensemble structures of the complex. Thr(8), Pro(10), Lys(38), Val(39), Val(40), and Pro(69) in alpha-bungarotoxin and Tyr(189), Tyr(190), Thr(191), Cys(192), Asp(195), and Thr(196) in the peptide participate in major intermolecular contacts. A comparison of the free and bound alpha-bungarotoxin structures reveals significant conformational rearrangements in flexible regions of alpha-bungarotoxin, mainly loops I, II, and the C-terminal tail. Furthermore, several of the calculated structures suggest that cation-pi interactions may be involved in binding. The root mean square deviation of the polypeptide backbone in the complex is 2.07 A. This structure provides, to date, the highest resolution description of the contacts between a prototypic alpha-neurotoxin and its cognate recognition sequence.

PubMed: 11312275
DOI: 10.1074/jbc.M102300200

実験手法

SOLUTION NMR