1e4t: Difference between revisions
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<StructureSection load='1e4t' size='340' side='right'caption='[[1e4t]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1e4t' size='340' side='right'caption='[[1e4t]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == 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 [ | <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'>[ | </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> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/DEFB7_MOUSE DEFB7_MOUSE]] Has bactericidal activity. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 17:30, 29 December 2021
Solution structure of the mouse defensin mBD-7Solution structure of the mouse defensin mBD-7
Structural highlights
Function[DEFB7_MOUSE] Has bactericidal activity. Publication Abstract from PubMedDefensins 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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