3L5U
Crystal structure of macrophage migration inhibitory factor (MIF) with benzothiazole inhibitor at 1.90A resolution
Summary for 3L5U
| Entry DOI | 10.2210/pdb3l5u/pdb |
| Related | 3L5P 3L5R 3L5S 3L5T 3L5V |
| Descriptor | Macrophage migration inhibitory factor, 6-HYDROXY-1,3-BENZOTHIAZOLE-2-SULFONAMIDE, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | protein-ligand complex, cytokine, cytoplasm, immune response, inflammatory response, innate immunity, isomerase, phosphoprotein, secreted, acetylation |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted : P14174 |
| Total number of polymer chains | 3 |
| Total formula weight | 41257.61 |
| Authors | McLean, L.,Zhang, Y. (deposition date: 2009-12-22, release date: 2010-03-09, Last modification date: 2023-09-06) |
| Primary citation | McLean, L.R.,Zhang, Y.,Li, H.,Choi, Y.M.,Han, Z.,Vaz, R.J.,Li, Y. Fragment screening of inhibitors for MIF tautomerase reveals a cryptic surface binding site. Bioorg.Med.Chem.Lett., 20:1821-1824, 2010 Cited by PubMed Abstract: In the course of a fragment screening campaign by in silico docking followed by X-ray crystallography, a novel binding site for migration inhibitory factor (MIF) inhibitors was demonstrated. The site is formed by rotation of the side-chain of Tyr-36 to reveal a surface binding site in MIF that is hydrophobic and surrounded by aromatic side-chain residues. The crystal structures of two small inhibitors that bind to this site and of a quinolinone inhibitor, that spans the canonical deep pocket near Pro-1 and the new surface binding site, have been solved. These results suggest new opportunities for structure-based design of MIF inhibitors. PubMed: 20185308DOI: 10.1016/j.bmcl.2010.02.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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