1dfn | pdb_00001dfn
CRYSTAL STRUCTURE OF DEFENSIN HNP-3, AN AMPHIPHILIC DIMER: MECHANISMS OF MEMBRANE PERMEABILIZATION
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Overview
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.
Disease
Known disease associated with this structure: Mental retardation, X-linked, South African type OMIM:[300243]
About this Structure
1DFN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization., Hill CP, Yee J, Selsted ME, Eisenberg D, Science. 1991 Mar 22;251(5000):1481-5. PMID:2006422
Page seeded by OCA on Mon Nov 12 16:31:51 2007
