1DFN

CRYSTAL STRUCTURE OF DEFENSIN HNP-3, AN AMPHIPHILIC DIMER: MECHANISMS OF MEMBRANE PERMEABILIZATION

Summary for 1DFN

• Entry DOI: 10.2210/pdb1dfn/pdb
• Descriptor: DEFENSIN HNP-3 (2 entities in total)
• Functional Keywords: defensin
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P59665
• Total number of polymer chains: 2
• Total formula weight: 6992.24

Authors

Hill, C.P.,Yee, J.,Selsted, M.E.,Eisenberg, D. (deposition date: 1991-01-18, release date: 1992-07-15, Last modification date: 2024-10-23)

Primary citation

Hill, C.P.,Yee, J.,Selsted, M.E.,Eisenberg, D.
Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization.
Science, 251:1481-1485, 1991

PubMed 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.

PubMed: 2006422

Experimental method

X-RAY DIFFRACTION (1.9 Å)