1E4T
Solution structure of the mouse defensin mBD-7
1E4T の概要
エントリーDOI | 10.2210/pdb1e4t/pdb |
分子名称 | Beta-defensin 7 (1 entity in total) |
機能のキーワード | defensin, mouse |
由来する生物種 | Mus musculus (Mouse) |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 4355.17 |
構造登録者 | Bauer, F.,Schweimer, K.,Kluver, E.,Adermann, K.,Forssmann, W.G.,Roesch, P.,Sticht, H. (登録日: 2000-07-12, 公開日: 2001-07-12, 最終更新日: 2024-10-16) |
主引用文献 | 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 主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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