1E4R
Solution structure of the mouse defensin mBD-8
Summary for 1E4R
| Entry DOI | 10.2210/pdb1e4r/pdb |
| Descriptor | Beta-defensin 8 (1 entity in total) |
| Functional Keywords | defensin, mouse |
| Biological source | Mus musculus (Mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 3849.60 |
| Authors | Bauer, F.,Schweimer, K.,Kluver, E.,Adermann, K.,Forssmann, W.G.,Roesch, P.,Sticht, H. (deposition date: 2000-07-12, release date: 2001-07-12, Last modification date: 2018-06-20) |
| Primary citation | Bauer, F.,Schweimer, K.,Kluver, E.,Conejo-Garcia, J.R.,Forssmann, W.G.,Rosch, 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., 10:2470-2479, 2001 Cited by PubMed Abstract: 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. PubMed: 11714914DOI: 10.1110/ps.24401 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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