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Structure determination of human and murine beta-defensins reveals structural conservation in the absence of significant sequence similarity.

Publication ,  Journal Article
Bauer, F; Schweimer, K; Klüver, E; Conejo-Garcia, JR; Forssmann, WG; Rösch, P; Adermann, K; Sticht, H
Published in: Protein Sci
December 2001

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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Published In

Protein Sci

DOI

ISSN

0961-8368

Publication Date

December 2001

Volume

10

Issue

12

Start / End Page

2470 / 2479

Location

United States

Related Subject Headings

  • beta-Defensins
  • Sequence Homology, Amino Acid
  • Protein Structure, Tertiary
  • Protein Structure, Secondary
  • Protein Folding
  • Protein Conformation
  • Peptides
  • Molecular Sequence Data
  • Models, Molecular
  • Mice
 

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Bauer, F., Schweimer, K., Klüver, E., Conejo-Garcia, J. R., Forssmann, W. G., Rösch, P., … Sticht, H. (2001). Structure determination of human and murine beta-defensins reveals structural conservation in the absence of significant sequence similarity. Protein Sci, 10(12), 2470–2479. https://doi.org/10.1110/ps.24401
Bauer, F., K. Schweimer, E. Klüver, J. R. Conejo-Garcia, W. G. Forssmann, P. Rösch, K. Adermann, and H. Sticht. “Structure determination of human and murine beta-defensins reveals structural conservation in the absence of significant sequence similarity.Protein Sci 10, no. 12 (December 2001): 2470–79. https://doi.org/10.1110/ps.24401.
Bauer F, Schweimer K, Klüver E, Conejo-Garcia JR, Forssmann WG, Rösch P, et al. Structure determination of human and murine beta-defensins reveals structural conservation in the absence of significant sequence similarity. Protein Sci. 2001 Dec;10(12):2470–9.
Bauer, F., et al. “Structure determination of human and murine beta-defensins reveals structural conservation in the absence of significant sequence similarity.Protein Sci, vol. 10, no. 12, Dec. 2001, pp. 2470–79. Pubmed, doi:10.1110/ps.24401.
Bauer F, Schweimer K, Klüver E, Conejo-Garcia JR, Forssmann WG, Rösch P, Adermann K, Sticht H. Structure determination of human and murine beta-defensins reveals structural conservation in the absence of significant sequence similarity. Protein Sci. 2001 Dec;10(12):2470–2479.

Published In

Protein Sci

DOI

ISSN

0961-8368

Publication Date

December 2001

Volume

10

Issue

12

Start / End Page

2470 / 2479

Location

United States

Related Subject Headings

  • beta-Defensins
  • Sequence Homology, Amino Acid
  • Protein Structure, Tertiary
  • Protein Structure, Secondary
  • Protein Folding
  • Protein Conformation
  • Peptides
  • Molecular Sequence Data
  • Models, Molecular
  • Mice