2OS5
Macrophage migration inhibitory factor from Ancylostoma ceylanicum
Summary for 2OS5
| Entry DOI | 10.2210/pdb2os5/pdb |
| Descriptor | AceMIF, SULFATE ION (3 entities in total) |
| Functional Keywords | macrophage migration inhibitory factor, cytokine, nematode, hookworm |
| Biological source | Ancylostoma ceylanicum |
| Total number of polymer chains | 4 |
| Total formula weight | 52948.85 |
| Authors | |
| Primary citation | Cho, Y.,Jones, B.F.,Vermeire, J.J.,Leng, L.,DiFedele, L.,Harrison, L.M.,Xiong, H.,Kwong, Y.K.,Chen, Y.,Bucala, R.,Lolis, E.,Cappello, M. Structural and functional characterization of a secreted hookworm Macrophage Migration Inhibitory Factor (MIF) that interacts with the human MIF receptor CD74. J.Biol.Chem., 282:23447-23456, 2007 Cited by PubMed Abstract: Hookworms, parasitic nematodes that infect nearly one billion people worldwide, are a major cause of anemia and malnutrition. We hypothesize that hookworms actively manipulate the host immune response through the production of specific molecules designed to facilitate infection by larval stages and adult worm survival within the intestine. A full-length cDNA encoding a secreted orthologue of the human cytokine, Macrophage Migration Inhibitory Factor (MIF) has been cloned from the hookworm Ancylostoma ceylanicum. Elucidation of the three-dimensional crystal structure of recombinant AceMIF (rAceMIF) revealed an overall structural homology with significant differences in the tautomerase sites of the human and hookworm proteins. The relative bioactivities of human and hookworm MIF proteins were compared using in vitro assays of tautomerase activity, macrophage migration, and binding to MIF receptor CD74. The activity of rAceMIF was not inhibited by the ligand ISO-1, which was previously determined to be an inhibitor of the catalytic site of human MIF. These data define unique immunological, structural, and functional characteristics of AceMIF, thereby establishing the potential for selectively inhibiting the hookworm cytokine as a means of reducing parasite survival and disease pathogenesis. PubMed: 17567581DOI: 10.1074/jbc.M702950200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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