1dfn
From Proteopedia
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| - | [[Image:1dfn.jpg|left|200px]] | + | [[Image:1dfn.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF DEFENSIN HNP-3, AN AMPHIPHILIC DIMER: MECHANISMS OF MEMBRANE PERMEABILIZATION''' | + | {{Structure |
| + | |PDB= 1dfn |SIZE=350|CAPTION= <scene name='initialview01'>1dfn</scene>, resolution 1.9Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF DEFENSIN HNP-3, AN AMPHIPHILIC DIMER: MECHANISMS OF MEMBRANE PERMEABILIZATION''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DFN is a [ | + | 1DFN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DFN OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/2006422 2006422] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: defensin]] | [[Category: defensin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:37:50 2008'' |
Revision as of 08:37, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF DEFENSIN HNP-3, AN AMPHIPHILIC DIMER: MECHANISMS OF MEMBRANE PERMEABILIZATION
Contents |
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 Thu Mar 20 10:37:50 2008
