2AP7

Solution structure of bombinin H2 in DPC micelles

Summary for 2AP7

• Entry DOI: 10.2210/pdb2ap7/pdb
• Related: 2AP8
• NMR Information: BMRB: 6774
• Descriptor: Bombinin H2 (1 entity in total)
• Functional Keywords: alpha helix, dpc micelle, antibiotic
• Biological source: Bombina variegata
• Total number of polymer chains: 1
• Total formula weight: 1920.43

Authors

Zangger, K.,Jilek, A.,Khatai, L. (deposition date: 2005-08-15, release date: 2006-08-01, Last modification date: 2024-05-15)

Primary citation

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

Experimental method

SOLUTION NMR