Science. 1991 Mar 22;251(5000):1481-5.

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

Hill CP, Yee J, Selsted ME, Eisenberg D.

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Eisenberg, Molecular Biology Institute, Los Angeles, CA.

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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Structures reported by this article

Crystal Structure Of Defensin Hnp-3, An Amphiphilic Dimer: Mechanisms Of Membrane Permeabilization

PDB: 1DFN

Source: Homo sapiens

Method: X-Ray Diffraction

Resolution: 1.9 Å

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