Solution structure of a defense peptide from wheat with a 10-cysteine motif

► WAMP-1a is a defense peptide from the wheat Triticum kiharae. ► NMR spectroscopy detects the hevein-type fold. ► Absence of a conserved serine abrogates the peptide binding to chitooligosaccharides. ► The peptide displays antibacterial and antifungal activities. ► Amphiphilicity of the peptide may be a key to its function.