1e4s

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[[Image:1e4s.jpg|left|200px]]
 
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{{Structure
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==Solution structure of the human defensin hBD-1==
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|PDB= 1e4s |SIZE=350|CAPTION= <scene name='initialview01'>1e4s</scene>
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<StructureSection load='1e4s' size='340' side='right'caption='[[1e4s]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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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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|ACTIVITY=
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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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|GENE=
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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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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e4s OCA], [http://www.ebi.ac.uk/pdbsum/1e4s PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e4s RCSB]</span>
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[https://www.uniprot.org/uniprot/DEFB1_HUMAN DEFB1_HUMAN] Has bactericidal activity (By similarity).
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}}
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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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'''SOLUTION STRUCTURE OF THE HUMAN DEFENSIN HBD-1'''
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==See Also==
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*[[Defensin 3D structures|Defensin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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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==About this Structure==
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1E4S 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=1E4S OCA].
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/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://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:55:08 2008''
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Current revision

Solution structure of the human defensin hBD-1

PDB ID 1e4s

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OCA

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