A hemocyanin-derived antimicrobial peptide from the penaeid shrimp adopts an alpha-helical structure that specifically permeabilizes fungal membranes.
Petit, V.W., Rolland, J.L., Blond, A., Cazevieille, C., Djediat, C., Peduzzi, J., Goulard, C., Bachere, E., Dupont, J., Destoumieux-Garzon, D., Rebuffat, S.(2015) Biochim Biophys Acta 1860: 557-568
- PubMed: 26708991 
- DOI: https://doi.org/10.1016/j.bbagen.2015.12.010
- Primary Citation of Related Structures:  
2N1C, 2N30 - PubMed Abstract: 
Hemocyanins are respiratory proteins with multiple functions. In diverse crustaceans hemocyanins can release histidine-rich antimicrobial peptides in response to microbial challenge. In penaeid shrimp, strictly antifungal peptides are released from the C-terminus of hemocyanins.
Organizational Affiliation: 
Laboratory Molécules de Communication et Adaptation des Microorganismes (MCAM, UMR 7245), Muséum national d'Histoire naturelle (MNHN), Centre national de la Recherche scientifique (CNRS), Sorbonne Universités, 75005 Paris, France.