Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization.

Academic Article


  • Defensins (molecular weight 3500 to 4000) act in the mammalian immune response by permeabilizing the plasma membranes of a broad spectrum of target organisms, including bacteria, fungi, and enveloped viruses. The high-resolution crystal structure of defensin HNP-3 (1.9 angstrom resolution, R factor 0.19) reveals a dimeric beta sheet that has an architecture very different from other lytic peptides. The dimeric assembly suggests mechanisms by which defensins might bind to and permeabilize the lipid bilayer.
  • Authors

    Published In

  • Science  Journal
  • Keywords

  • Amino Acid Sequence, Animals, Blood Proteins, Cell Membrane Permeability, Crystallography, Defensins, Guinea Pigs, Humans, Macromolecular Substances, Membrane Proteins, Models, Molecular, Molecular Sequence Data, Molecular Structure, Protein Conformation, Rabbits, Rats, Structure-Activity Relationship, X-Ray Diffraction, alpha-Defensins
  • Digital Object Identifier (doi)

    Author List

  • Hill CP; Yee J; Selsted ME; Eisenberg D
  • Start Page

  • 1481
  • End Page

  • 1485
  • Volume

  • 251
  • Issue

  • 5000