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1dfn

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(New page: 200px<br /> <applet load="1dfn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dfn, resolution 1.9&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1dfn.gif|left|200px]]<br />
 
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<applet load="1dfn" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dfn, resolution 1.9&Aring;" />
 
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'''CRYSTAL STRUCTURE OF DEFENSIN HNP-3, AN AMPHIPHILIC DIMER: MECHANISMS OF MEMBRANE PERMEABILIZATION'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF DEFENSIN HNP-3, AN AMPHIPHILIC DIMER: MECHANISMS OF MEMBRANE PERMEABILIZATION==
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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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<StructureSection load='1dfn' size='340' side='right'caption='[[1dfn]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dfn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The June 2013 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Dermcidin'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2013_6 10.2210/rcsb_pdb/mom_2013_6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DFN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DFN FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dfn OCA], [https://pdbe.org/1dfn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dfn RCSB], [https://www.ebi.ac.uk/pdbsum/1dfn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dfn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DEF3_HUMAN 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.<ref>PMID:15616305</ref> <ref>PMID:2006422</ref> <ref>PMID:15894545</ref> <ref>PMID:17452329</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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==Disease==
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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<ref>PMID:2006422</ref>
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Known disease associated with this structure: Mental retardation, X-linked, South African type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300243 300243]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1DFN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DFN OCA].
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</div>
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<div class="pdbe-citations 1dfn" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=2006422 2006422]
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*[[Defensin 3D structures|Defensin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Dermcidin]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Eisenberg, D.]]
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[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Hill, C.P.]]
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[[Category: Eisenberg D]]
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[[Category: Selsted, M.E.]]
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[[Category: Hill CP]]
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[[Category: Yee, J.]]
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[[Category: Selsted ME]]
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[[Category: defensin]]
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[[Category: Yee J]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:31:51 2007''
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Current revision

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

PDB ID 1dfn

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