2AP8

Solution structure of bombinin H4 in DPC micelles

2AP8 の概要

• エントリーDOI: 10.2210/pdb2ap8/pdb
• 関連するPDBエントリー: 2AP7
• NMR情報: BMRB: 6775
• 分子名称: bombinin H4 (1 entity in total)
• 機能のキーワード: alpha-helix, dpc micelle, d-ile, antibiotic
• 由来する生物種: Bombina variegata
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1920.43

構造登録者

Zangger, K.,Jilek, A.,Khatai, L. (登録日: 2005-08-15, 公開日: 2006-08-01, 最終更新日: 2024-10-23)

主引用文献

Zangger, K.,Gossler, R.,Khatai, L.,Lohner, K.,Jilek, A.
Structures of the glycine-rich diastereomeric peptides bombinin H2 and H4.
Toxicon, 52:246-254, 2008

PubMed Abstract: Skin secretions of the European frog Bombina variegata contain a family of hydrophobic peptides, called bombinins H, which probably play a role in the defense against microbes. These peptides are rich in glycine (25%), which may allow structural polymorphism. Indeed, there is increasing evidence that bombinin H can, dependent on the environment, adopt different conformations. Moreover, some of these peptides contain a d-amino acid; the bombinins H2 and H4 differ from each other in that they contain either L-Ile or D-allo-Ile at position 2. In this paper we report the solution structure obtained by using NMR techniques of the mainly helical conformation, which these peptides adopt upon binding to the bilayer mimetics SDS and DPC. A glycine ridge is exposed at one side of the helix and may provide a helix-helix interaction site. In this respect, the structure of bombinin H resembles the influenza hemagglutinin fusion peptide and the helical conformer of Alzheimer peptide Abeta(25-40). Neither structure nor orientation of bombinin H are affected by the chiral inversion. Environmental conditions can trigger self-aggregation of bombinin H in solution due to hydrophobic interaction. Under these conditions the stereochemistry of the randomly ordered N-terminal segment modulates the preference to fold into a particular conformation.

PubMed: 18586045
DOI: 10.1016/j.toxicon.2008.05.011

実験手法

SOLUTION NMR