1IK8

NMR structure of Alpha-Bungarotoxin

1IK8 の概要

• エントリーDOI: 10.2210/pdb1ik8/pdb
• 関連するPDBエントリー: 1HN7 1HOY
• 分子名称: LONG NEUROTOXIN 1 (1 entity in total)
• 機能のキーワード: alpha-bungarotoxin, toxin, nicotinic-acetilcholine receptor
• 由来する生物種: Bungarus multicinctus (many-banded krait)
• 細胞内の位置: Secreted: P60615
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8005.28

構造登録者

Niccolai, N.,Ciutti, A.,Spiga, O. (登録日: 2001-05-03, 公開日: 2001-05-16, 最終更新日: 2024-10-09)

主引用文献

Scarselli, M.,Spiga, O.,Ciutti, A.,Bernini, A.,Bracci, L.,Lelli, B.,Lozzi, L.,Calamandrei, D.,Di Maro, D.,Klein, S.,Niccolai, N.
NMR structure of alpha-bungarotoxin free and bound to a mimotope of the nicotinic acetylcholine receptor.
Biochemistry, 41:1457-1463, 2002

PubMed Abstract: A combinatorial library approach was used to produce synthetic peptides mimicking the snake neurotoxin binding site of nicotinic receptors. Among the sequences, which inhibited binding of alpha-bungarotoxin to muscle and neuronal nicotinic receptors, HRYYESSLPWYPD, a 14-amino acid peptide with considerably higher toxin-binding affinity than the other synthesized peptides, was selected, and the structure of its complex with the toxin was analyzed by NMR. Comparison of the solution structure of the free toxin and its complex with this peptide indicated that complex formation induced extensive conformational rearrangements mainly at finger II and the carboxy terminus of the protein. The peptidyl residues P10 and Y4 seemed to be critical for peptide folding and complex stability, respectively. The latter residue of the peptide strongly interacted with the protein by entering a small pocket delimited by D30, C33, S34, R36, and V39 toxin side chains.

PubMed: 11814338
DOI: 10.1021/bi011012f

実験手法

SOLUTION NMR