1dfn

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{{STRUCTURE_1dfn| PDB=1dfn | SCENE= }}
{{STRUCTURE_1dfn| PDB=1dfn | SCENE= }}
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'''CRYSTAL STRUCTURE OF DEFENSIN HNP-3, AN AMPHIPHILIC DIMER: MECHANISMS OF MEMBRANE PERMEABILIZATION'''
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===CRYSTAL STRUCTURE OF DEFENSIN HNP-3, AN AMPHIPHILIC DIMER: MECHANISMS OF MEMBRANE PERMEABILIZATION===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 2006422 is the PubMed ID number.
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{{ABSTRACT_PUBMED_2006422}}
==About this Structure==
==About this Structure==
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[[Category: Yee, J.]]
[[Category: Yee, J.]]
[[Category: Defensin]]
[[Category: Defensin]]
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Revision as of 20:00, 30 June 2008

Image:1dfn.png

Template:STRUCTURE 1dfn

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

Template:ABSTRACT PUBMED 2006422

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

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