1e4s

<StructureSection load='1e4s' size='340' side='right'caption='[[1e4s]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1e4s]] is a 1 chain structure. 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>

</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=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>

[[https://www.uniprot.org/uniprot/DEFB1_HUMAN DEFB1_HUMAN]] Has bactericidal activity (By similarity).

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== 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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1e4s" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Adermann, K]]

[[Category: Bauer, F]]

[[Category: Forssmann, W G]]

[[Category: Kluver, E]]

[[Category: Roesch, P]]

[[Category: Schweimer, K]]

[[Category: Sticht, H]]

[[Category: Human]]