1dfn: Difference between revisions
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New page: left|200px<br /> <applet load="1dfn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dfn, resolution 1.9Å" /> '''CRYSTAL STRUCTURE OF... |
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== | ==CRYSTAL STRUCTURE OF DEFENSIN HNP-3, AN AMPHIPHILIC DIMER: MECHANISMS OF MEMBRANE PERMEABILIZATION== | ||
Defensins (molecular weight 3500 to 4000) act in the mammalian immune | <StructureSection load='1dfn' size='340' side='right'caption='[[1dfn]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | |||
<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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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> | |||
</table> | |||
== Function == | |||
[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> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:2006422</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1dfn" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Defensin 3D structures|Defensin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Dermcidin]] | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: RCSB PDB Molecule of the Month]] | ||
[[Category: | [[Category: Eisenberg D]] | ||
[[Category: | [[Category: Hill CP]] | ||
[[Category: | [[Category: Selsted ME]] | ||
[[Category: | [[Category: Yee J]] | ||
Latest revision as of 07:19, 23 October 2024
CRYSTAL STRUCTURE OF DEFENSIN HNP-3, AN AMPHIPHILIC DIMER: MECHANISMS OF MEMBRANE PERMEABILIZATION
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