Reports

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

Science  22 Mar 1991:
Vol. 251, Issue 5000, pp. 1481-1485
DOI: 10.1126/science.2006422

Abstract

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.

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