3jtu | pdb_00003jtu

Crystal structure of macrophage migration inhibitory factor (mif) with hydroxyquinoline inhibitor 708 at 1.86a resolution

spinqualitylabelsall models 3jtu, resolution 1.86Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3jtu is a 3 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4, ZIN Related: 3jsf, 3jsg Gene: GLIF, MIF, MMIF (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Disease [MIF_HUMAN] Genetic variations in MIF are associated with susceptibility to rheumatoid arthritis systemic juvenile (RASJ) [MIM:604302]. An inflammatory articular disorder with systemic-onset beginning before the age of 16. It represents a subgroup of juvenile arthritis associated with severe extraarticular features and occasionally fatal complications. During active phases of the disorder, patients display a typical daily spiking fever, an evanescent macular rash, lymphadenopathy, hepatosplenomegaly, serositis, myalgia and arthritis. Function [MIF_HUMAN] Pro-inflammatory cytokine. Involved in the innate immune response to bacterial pathogens. The expression of MIF at sites of inflammation suggests a role as mediator in regulating the function of macrophages in host defense. Counteracts the anti-inflammatory activity of glucocorticoids. Has phenylpyruvate tautomerase and dopachrome tautomerase activity (in vitro), but the physiological substrate is not known. It is not clear whether the tautomerase activity has any physiological relevance, and whether it is important for cytokine activity. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Biochemical and X-ray crystallographic studies confirmed that hydroxyquinoline derivatives identified by virtual screening were actually covalent inhibitors of the MIF tautomerase. Adducts were formed by N-alkylation of the Pro-1 at the catalytic site with a loss of an amino group of the inhibitor. Discovery of covalent inhibitors for MIF tautomerase via cocrystal structures with phantom hits from virtual screening.,McLean LR, Zhang Y, Li H, Li Z, Lukasczyk U, Choi YM, Han Z, Prisco J, Fordham J, Tsay JT, Reiling S, Vaz RJ, Li Y Bioorg Med Chem Lett. 2009 Dec 1;19(23):6717-20. Epub 2009 Oct 1. PMID:19836948 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Macrophage inhibitory factor

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