8UR2
Crystal Structure of macrophage migration inhibitory factor (MIF) from Trichomonas vaginalis (I41 form)
Summary for 8UR2
| Entry DOI | 10.2210/pdb8ur2/pdb |
| Descriptor | MACROPHAGE MIGRATION INHIBITORY FACTOR, IODIDE ION, PYRUVIC ACID, ... (4 entities in total) |
| Functional Keywords | ssgcid, structural genomics, seattle structural genomics center for infectious disease, macrophage migration inhibitory factor, cytokine |
| Biological source | Trichomonas vaginalis G3 |
| Total number of polymer chains | 6 |
| Total formula weight | 89271.75 |
| Authors | Seattle Structural Genomics Center for Infectious Disease,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2023-10-25, release date: 2023-11-08, Last modification date: 2024-12-11) |
| Primary citation | Srivastava, A.,Nair, A.,Dawson, O.C.O.,Gao, R.,Liu, L.,Craig, J.K.,Battaile, K.P.,Harmon, E.K.,Barrett, L.K.,Van Voorhis, W.C.,Subramanian, S.,Myler, P.J.,Lovell, S.,Asojo, O.A.,Darwiche, R. Structures of Trichomonas vaginalis macrophage migratory inhibitory factor. Acta Crystallogr.,Sect.F, 80:341-347, 2024 Cited by PubMed Abstract: The unicellular parasitic protozoan Trichomonas vaginalis causes trichomoniasis, the most prevalent nonviral sexually transmitted disease globally. T. vaginalis evades host immune responses by producing homologs of host proteins, including cytokines such as macrophage migration inhibitory factor. T. vaginalis macrophage migration inhibitory factor (TvMIF) helps to facilitate the survival of T. vaginalis during nutritional stress conditions, increases prostate cell proliferation and invasiveness, and induces inflammation-related cellular pathways, thus mimicking the ability of human MIF to increase inflammation and cell proliferation. The production, crystallization and three structures of N-terminally hexahistidine-tagged TvMIF reveal a prototypical MIF trimer with a topology similar to that of human homologs (hMIF-1 and hMIF-2). The N-terminal tag obscures the expected pyruvate-binding site. The similarity of TvMIF to its human homologs can be exploited for structure-based drug discovery. PubMed: 39601418DOI: 10.1107/S2053230X24011105 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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