1e4r: Difference between revisions
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{{STRUCTURE_1e4r| PDB=1e4r | SCENE= }} | |||
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'''SOLUTION STRUCTURE OF THE MOUSE DEFENSIN MBD-8''' | '''SOLUTION STRUCTURE OF THE MOUSE DEFENSIN MBD-8''' | ||
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[[Category: Schweimer, K.]] | [[Category: Schweimer, K.]] | ||
[[Category: Sticht, H.]] | [[Category: Sticht, H.]] | ||
[[Category: | [[Category: Defensin]] | ||
[[Category: | [[Category: Mouse]] | ||
[[Category: | [[Category: Nmr structure]] | ||
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Revision as of 14:39, 2 May 2008
SOLUTION STRUCTURE OF THE MOUSE DEFENSIN MBD-8
OverviewOverview
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.
About this StructureAbout this Structure
1E4R is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Fri May 2 14:39:38 2008