Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization |
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Authors: | C P Hill J Yee M E Selsted D Eisenberg |
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Institution: | Eisenberg, Molecular Biology Institute, Los Angeles, CA. |
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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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