1dfn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:19, 23 October 2024) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1dfn.jpg|left|200px]]
 
-
{{Structure
+
==CRYSTAL STRUCTURE OF DEFENSIN HNP-3, AN AMPHIPHILIC DIMER: MECHANISMS OF MEMBRANE PERMEABILIZATION==
-
|PDB= 1dfn |SIZE=350|CAPTION= <scene name='initialview01'>1dfn</scene>, resolution 1.9&Aring;
+
<StructureSection load='1dfn' size='340' side='right'caption='[[1dfn]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND=
+
<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>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-
|GENE=
+
<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>
-
|DOMAIN=
+
</table>
-
|RELATEDENTRY=
+
== Function ==
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dfn OCA], [http://www.ebi.ac.uk/pdbsum/1dfn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dfn RCSB]</span>
+
[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'''
+
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1dfn" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
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.
+
*[[Defensin 3D structures|Defensin 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
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].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
[[Category: Dermcidin]]
-
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: Large Structures]]
-
[[Category: Eisenberg, D.]]
+
[[Category: RCSB PDB Molecule of the Month]]
-
[[Category: Hill, C P.]]
+
[[Category: Eisenberg D]]
-
[[Category: Selsted, M E.]]
+
[[Category: Hill CP]]
-
[[Category: Yee, J.]]
+
[[Category: Selsted ME]]
-
[[Category: defensin]]
+
[[Category: Yee J]]
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:40:43 2008''
+

Current revision

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

PDB ID 1dfn

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dfn"
Personal tools