Crystal Structure of Defensin HNP-3, an Amphiphilic Dimer: Mechanisms of Membrane Permeabilization

DOI Web Site 7 Citations
  • Christopher P. Hill
    Molecular Biology Institute and Departments of Chemistry and Biochemistry, University of California, Los Angeles, CA 90024- 1570.
  • Jeff Yee
    Molecular Biology Institute and Departments of Chemistry and Biochemistry, University of California, Los Angeles, CA 90024- 1570.
  • Michael E. Selsted
    Departments of Medicine and Pathology, University of California, Los Angeles, CA 90024-1732.
  • David Eisenberg
    Molecular Biology Institute and Departments of Chemistry and Biochemistry, University of California, Los Angeles, CA 90024- 1570.

Abstract

<jats:p> 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, <jats:italic>R</jats:italic> factor 0.19) reveals a dimeric β 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. </jats:p>

Journal

  • Science

    Science 251 (5000), 1481-1485, 1991-03-22

    American Association for the Advancement of Science (AAAS)

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