View source for 8uz4


==Crystal Structure of macrophage migration inhibitory factor (MIF) from Trichomonas vaginalis (Apo, P41212 form)==
<StructureSection load='8uz4' size='340' side='right'caption='[[8uz4]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8uz4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichomonas_vaginalis_G3 Trichomonas vaginalis G3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8UZ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8UZ4 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8uz4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8uz4 OCA], [https://pdbe.org/8uz4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8uz4 RCSB], [https://www.ebi.ac.uk/pdbsum/8uz4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8uz4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A2DXT4_TRIV3 A2DXT4_TRIV3] 
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== Publication Abstract from PubMed ==
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.

Structures of Trichomonas vaginalis macrophage migratory inhibitory factor.,Srivastava A, Nair A, Dawson OCO, Gao R, Liu L, Craig JK, Battaile KP, Harmon EK, Barrett LK, Van Voorhis WC, Subramanian S, Myler PJ, Lovell S, Asojo OA, Darwiche R Acta Crystallogr F Struct Biol Commun. 2024 Dec 1;80(Pt 12):341-7. doi: , 10.1107/S2053230X24011105. PMID:39601418<ref>PMID:39601418</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 8uz4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Trichomonas vaginalis G3]]
[[Category: Structural genomic]]