3GAD
Structure of apomif
3GAD の概要
| エントリーDOI | 10.2210/pdb3gad/pdb |
| 関連するPDBエントリー | 3GAC |
| 分子名称 | Macrophage migration inhibitory factor-like protein, SULFATE ION, ACETIC ACID, ... (4 entities in total) |
| 機能のキーワード | macrophage migration inhibitory factor, cytokine |
| 由来する生物種 | Plasmodium yoelii yoelii |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 78568.17 |
| 構造登録者 | |
| 主引用文献 | Shao, D.,Zhong, X.,Zhou, Y.-F.,Han, Z.,Lin, Y.,Wang, Z.,Bu, L.,Zhang, L.,Su, X.-D.,Wang, H. Structural and functional comparison of MIF ortholog from Plasmodium yoelii with MIF from its rodent host Mol.Immunol., 47:726-737, 2010 Cited by PubMed Abstract: Host-derived macrophage migration inhibitory factor (MIF) has been implicated in the pathogenesis of malaria infection, especially in malarial anemia. Although two Plasmodium parasite-derived MIF orthologs, Plasmodium falciparum MIF and P. berghei MIF were identified recently, the crystal structure and the precise roles of Plasmodium-derived MIFs, particularly in combination with the host MIF, remain unknown. In this study, we identified another MIF ortholog from a rodent-specific P. yoelii (PyMIF). This molecule shares a conserved three-dimensional structure with murine MIF (MmMIF), but with a different substrate binding pattern and much lower tautomerase activity. It could activate host cells via several signaling pathways in vitro, and inhibiting macrophage apoptosis, also similarly to MmMIF. However, we found that PyMIF and MmMIF acted synergistically to activate the MAPK-ERK1/2 signaling pathway at very low concentration but acted antagonistically at higher concentration. Furthermore, we detected PyMIF in the sera of infected mice and found that injection of recombinant PyMIF (rPyMIF) during infection could up-regulate several pro-inflammatory cytokines in vivo and slightly delay the death of infected mice. These data suggest that PyMIF modulates host immune responses together with host MIF and has potential to prolong parasitemia or the chronicity of malaria infection. PubMed: 20004020DOI: 10.1016/j.molimm.2009.10.037 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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