View source for 1e4t


==Solution structure of the mouse defensin mBD-7==
<StructureSection load='1e4t' size='340' side='right'caption='[[1e4t]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1e4t]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E4T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E4T 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=1e4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e4t OCA], [https://pdbe.org/1e4t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e4t RCSB], [https://www.ebi.ac.uk/pdbsum/1e4t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e4t ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/DEFB7_MOUSE DEFB7_MOUSE]] Has bactericidal activity. 
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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>
</div>
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==See Also==
*[[Defensin 3D structures|Defensin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Adermann, K]]
[[Category: Bauer, F]]
[[Category: Forssmann, W G]]
[[Category: Kluver, E]]
[[Category: Roesch, P]]
[[Category: Schweimer, K]]
[[Category: Sticht, H]]
[[Category: Defensin]]
[[Category: Mouse]]