1e4q: Difference between revisions

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-[[Image:1e4q.png|left|200px]]
-{{STRUCTURE_1e4q|  PDB=1e4q  |  SCENE=  }}
+==Solution structure of the human defensin hBD-2==
+<StructureSection load='1e4q' size='340' side='right'caption='[[1e4q]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1e4q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E4Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E4Q FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=1e4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e4q OCA], [https://pdbe.org/1e4q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e4q RCSB], [https://www.ebi.ac.uk/pdbsum/1e4q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e4q ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/DFB4A_HUMAN DFB4A_HUMAN]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Defensins are cationic and cysteine-rich peptides that play a crucial role in the host defense against microorganisms of many organisms by their capability to permeabilize bacterial membranes. The low sequence similarity among the members of the large mammalian beta-defensin family suggests that their antimicrobial activity is largely independent of their primary structure. To investigate to what extent these defensins share a similar fold, the structures of the two human beta-defensins, hBD-1 and hBD-2, as well as those of two novel murine defensins, termed mBD-7 and mBD-8, were determined by nuclear magnetic resonance spectroscopy. All four defensins investigated share a striking similarity on the level of secondary and tertiary structure including the lack of a distinct hydrophobic core, suggesting that the fold is mainly stabilized by the presence of three disulfide bonds. In addition to the overall shape of the molecules, the ratio of solvent-exposed polar and hydrophobic side chains is also very similar among the four defensins investigated. It is significant that beta-defensins do not exhibit a common pattern of charged and hydrophobic residues on the protein surface and that the beta-defensin-specific fold appears to accommodate a wide range of different amino acids at most sequence positions. In addition to the implications for the mode of biological defensin actions, these findings are of particular interest because beta-defensins have been suggested as lead compounds for the development of novel peptide antibiotics for the therapy of infectious diseases.
-===SOLUTION STRUCTURE OF THE HUMAN DEFENSIN HBD-2===
+Structure determination of human and murine beta-defensins reveals structural conservation in the absence of significant sequence similarity.,Bauer F, Schweimer K, Kluver E, Conejo-Garcia JR, Forssmann WG, Rosch P, Adermann K, Sticht H Protein Sci. 2001 Dec;10(12):2470-9. PMID:11714914<ref>PMID:11714914</ref>
-{{ABSTRACT_PUBMED_11714914}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 1e4q" style="background-color:#fffaf0;"></div>
-[[1e4q]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E4Q OCA].
 ==See Also==
-*[[Defensin|Defensin]]
+*[[Defensin 3D structures|Defensin 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:011714914</ref><references group="xtra"/>
+__TOC__
-[[Category: Adermann, K.]]
+</StructureSection>
-[[Category: Bauer, F.]]
+[[Category: Homo sapiens]]
-[[Category: Forssmann, W G.]]
+[[Category: Large Structures]]
-[[Category: Kluver, E.]]
+[[Category: Adermann K]]
-[[Category: Roesch, P.]]
+[[Category: Bauer F]]
-[[Category: Schweimer, K.]]
+[[Category: Forssmann WG]]
-[[Category: Sticht, H.]]
+[[Category: Kluver E]]
-[[Category: Defensin]]
+[[Category: Roesch P]]
-[[Category: Human]]
+[[Category: Schweimer K]]
+[[Category: Sticht H]]