1dfn

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

Structural highlights

1dfn is a 2 chain structure with sequence from Homo sapiens. The June 2013 RCSB PDB Molecule of the Month feature on Dermcidin by David Goodsell is 10.2210/rcsb_pdb/mom_2013_6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DEF3_HUMAN Defensin 2 and defensin 3 have antibiotic, fungicide and antiviral activities. Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane.[1] [2] [3] [4]

Publication Abstract from PubMed

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.

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[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
70 reviews cite this structure
Defensins: antimicrobial peptides of innate immunity.
Ganz et al. (2003)
69 more
191 other articles
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See Also

References

  1. ↑ Ericksen B, Wu Z, Lu W, Lehrer RI. Antibacterial activity and specificity of the six human {alpha}-defensins. Antimicrob Agents Chemother. 2005 Jan;49(1):269-75. PMID:15616305 doi:10.1128/AAC.49.1.269-275.2005
  2. ↑ Hill CP, Yee J, Selsted ME, Eisenberg D. Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization. Science. 1991 Mar 22;251(5000):1481-5. PMID:2006422
  3. ↑ Xie C, Prahl A, Ericksen B, Wu Z, Zeng P, Li X, Lu WY, Lubkowski J, Lu W. Reconstruction of the conserved beta-bulge in mammalian defensins using D-amino acids. J Biol Chem. 2005 Sep 23;280(38):32921-9. Epub 2005 May 13. PMID:15894545 doi:M503084200
  4. ↑ Zou G, de Leeuw E, Li C, Pazgier M, Li C, Zeng P, Lu WY, Lubkowski J, Lu W. Toward understanding the cationicity of defensins. Arg and Lys versus their noncoded analogs. J Biol Chem. 2007 Jul 6;282(27):19653-65. Epub 2007 Apr 23. PMID:17452329 doi:10.1074/jbc.M611003200
  5. ↑ Hill CP, Yee J, Selsted ME, Eisenberg D. Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization. Science. 1991 Mar 22;251(5000):1481-5. PMID:2006422

Contents


PDB ID 1dfn

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