Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization.
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.
Hill
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Eisenberg, Molecular Biology Institute, Los Angeles, CA.
Yee
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Selsted
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Eisenberg
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D000595:Amino Acid Sequence; D000818:Animals; D001798:Blood Proteins / Q000737:chemistry / Q000648:ultrastructure*; D002463:Cell Membrane Permeability; D003461:Crystallography; D023082:Defensins; D006168:Guinea Pigs; D006801:Humans; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000737:chemistry / Q000648:ultrastructure; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011487:Protein Conformation; D011817:Rabbits; D051381:Rats; D013329:Structure-Activity Relationship; D014961:X-Ray Diffraction; D023084:alpha-Defensins
D001798:Blood Proteins; D023082:Defensins; D046911:Macromolecular Substances; D008565:Membrane Proteins; D023084:alpha-Defensins; C406427:human neutrophil peptide 3