1e4s

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(New page: 200px<br /> <applet load="1e4s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e4s" /> '''SOLUTION STRUCTURE OF THE HUMAN DEFENSIN HB...)
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[[Image:1e4s.gif|left|200px]]<br />
 
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<applet load="1e4s" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1e4s" />
 
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'''SOLUTION STRUCTURE OF THE HUMAN DEFENSIN HBD-1'''<br />
 
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==Overview==
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==Solution structure of the human defensin hBD-1==
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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.
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<StructureSection load='1e4s' size='340' side='right'caption='[[1e4s]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1e4s]] 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=1E4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E4S FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e4s OCA], [https://pdbe.org/1e4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e4s RCSB], [https://www.ebi.ac.uk/pdbsum/1e4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e4s ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DEFB1_HUMAN DEFB1_HUMAN] Has bactericidal activity (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e4/1e4s_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1e4s ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1E4S 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=1E4S OCA].
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*[[Defensin 3D structures|Defensin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11714914 11714914]
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[[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: Adermann, K.]]
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[[Category: Adermann K]]
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[[Category: Bauer, F.]]
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[[Category: Bauer F]]
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[[Category: Forssmann, W.G.]]
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[[Category: Forssmann WG]]
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[[Category: Kluver, E.]]
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[[Category: Kluver E]]
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[[Category: Roesch, P.]]
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[[Category: Roesch P]]
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[[Category: Schweimer, K.]]
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[[Category: Schweimer K]]
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[[Category: Sticht, H.]]
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[[Category: Sticht H]]
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[[Category: defensin]]
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[[Category: human]]
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[[Category: nmr structure]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:39:51 2007''
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Current revision

Solution structure of the human defensin hBD-1

PDB ID 1e4s

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