Macrophage inhibitory factor

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<StructureSection load='2ooh' size='350' side='right' caption='Structure of human macrophage inhibitory factor trimer complex with inhibitor, glycerol and sulfate (PDB entry [[2ooh]])' scene=''>
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<StructureSection load='2ooh' size='350' side='right' caption='Structure of human macrophage inhibitory factor trimer complex with inhibitor, glycerol and sulfate (PDB entry [[2ooh]])' scene='55/551208/Cv/1'>
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== Function ==
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'''Macrophage inhibitory factor''' or '''Macrophage migration inhibitory factor''' (MIF) is an inflammatory cytokine. '''MIF2''' or '''D-dopachrome tautomerase''' or '''D-dopachrome decarboxylase''' is a pro-inflammatory cytokine which regulates the innate and adaptive immune response<ref>PMID:22507380</ref>. MIF is released to the blood stream upon stimulation of white blood cells by bacterial antigens<ref>PMID:11032394</ref>.
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'''Macrophage inhibitory factor''' (MIF) is an inflammatory cytokine. MIF is released to the blood stream upon stimulation of white blood cells by bacterial antigens. MIF contains two different catalytic sites. A phenylpyruvate tautomerase site is located in the N terminal. A disulfide reductase site is located in the tetrapeptide Cys-Ala-Leu-Cys in position 57-60.
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== Relevance ==
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</StructureSection>
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MIF plays a role in various solid and hematologic tumors<ref>PMID:19326434</ref>. MIF is overexpressed in various tumors and is suggested to be the molecular link between chronic inflammation and cancer. MIF has a role in skin inflammation, immune response, disease, tumorigenesis and wound healing<ref>PMID:15659324</ref>. MIF has a role in Alzheimer disease and its inhibition may prevent the disease onset<ref>PMID:20200619</ref>.
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== Structural highlights ==
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MIF contains two different catalytic sites. A phenylpyruvate tautomerase site is located in the N terminal. A <scene name='55/551208/Cv/5'>disulfide reductase site is located in the tetrapeptide Cys-Ala-Leu-Cys in position 57-60</scene>. The <scene name='55/551208/Cv/6'>inhibitor binds to the pro-inflammatory tautomerase site</scene><ref>PMID:17526494</ref>. Water molecules shown as red spheres.
==3D structures of macrophage inhibitory factor==
==3D structures of macrophage inhibitory factor==
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[[Macrophage inhibitory factor 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*macrophage inhibitory factor
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**[[1mif]] – MIF (mutant) – rat<BR />
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**[[1fim]], [[1gif]], [[1gd0]], [[3djh]] – hMIF – human<BR />
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**[[1cgq]], [[1p1g]], [[4etg]], [[4eui]], [[4evg]], [[4grn]], [[4gro]], [[4grp]], [[4grq]], [[4grr]], [[4gru]] – hMIF (mutant) <BR />
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**[[1mff]] – mMIF (mutant) – mouse<BR />
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**[[1hfo]] – MIF – ''Trichinella spiralis'' <BR />
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**[[1uiz]] – MIF – ''Xenopus laevis'' <BR />
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**[[2wkb]], [[2wkf]] – MIF – ''Plasmodium berghei'' <BR />
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**[[3t5s]] – MIF – ''Giardia lamblia''<BR />
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**[[4gum]] – MIF (mutant) – rhesus monkey<BR />
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**[[4dh4]] – MIF – ''Toxoplasma gondii'' <BR />
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*MIF complexes
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**[[1mfi]], [[2gdg]] – mMIF + inhibitor <BR />
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== References ==
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**[[1ca7]] – hMIF + hydroxyphenylpyruvate<BR />
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<references/>
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**[[3ijj]] – hMIF + hydroxyphenylpyruvate + inhibitor<BR />
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**[[1gcz]], [[1ljt]], [[2ooh]], [[2oow]], [[2ooz]], [[3b9s]], [[3jsf]], [[3jsg]], [[3jtu]], [[3l5p]], [[3l5r]], [[3l5s]], [[3l5t]], [[3l5u]], [[3l5v]], [[3ijg]], [[4f2k]], [[3smb]], [[3smc]], [[3wnr]], [[3wns]], [[3wnt]], [[4osf]], [[4p01]], [[4k9g]], [[4oyq]], [[4p0h]], [[4wr8]], [[4wrb]] – hMIF + inhibitor <BR />
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**[[3dji]] – hMIF + tylenol<BR />
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**[[3ce4]] – hMIF + PMSF<BR />
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**[[3hof]] – hMIF + cafeic acid<BR />
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**[[3u18]] – hMIF + Chicago sky blue<BR />
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**[[3rf4]], [[3rf5]] – MIF + inhibitor – ''Ancylostoma ceylanicum''<br />
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**[[4p7m]], [[4p7s]] – MIF + inhibitor – ''Plasmodium falciparum''<BR />
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}}
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[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Structure of human macrophage inhibitory factor trimer complex with inhibitor, glycerol and sulfate (PDB entry 2ooh)

Drag the structure with the mouse to rotate

References

  1. ↑ Merk M, Mitchell RA, Endres S, Bucala R. D-dopachrome tautomerase (D-DT or MIF-2): doubling the MIF cytokine family. Cytokine. 2012 Jul;59(1):10-7. doi: 10.1016/j.cyto.2012.03.014. Epub 2012 Apr 14. PMID:22507380 doi:http://dx.doi.org/10.1016/j.cyto.2012.03.014
  2. ↑ Nishihira J. Macrophage migration inhibitory factor (MIF): its essential role in the immune system and cell growth. J Interferon Cytokine Res. 2000 Sep;20(9):751-62. PMID:11032394 doi:http://dx.doi.org/10.1089/10799900050151012
  3. ↑ Bach JP, Deuster O, Balzer-Geldsetzer M, Meyer B, Dodel R, Bacher M. The role of macrophage inhibitory factor in tumorigenesis and central nervous system tumors. Cancer. 2009 May 15;115(10):2031-40. doi: 10.1002/cncr.24245. PMID:19326434 doi:http://dx.doi.org/10.1002/cncr.24245
  4. ↑ Shimizu T. Role of macrophage migration inhibitory factor (MIF) in the skin. J Dermatol Sci. 2005 Feb;37(2):65-73. PMID:15659324 doi:http://dx.doi.org/10.1016/j.jdermsci.2004.08.007
  5. ↑ Bacher M, Deuster O, Aljabari B, Egensperger R, Neff F, Jessen F, Popp J, Noelker C, Reese JP, Al-Abed Y, Dodel R. The role of macrophage migration inhibitory factor in Alzheimer's disease. Mol Med. 2010 Mar;16(3-4):116-21. doi: 10.2119/molmed.2009.00123. Epub 2010 Feb, 28. PMID:20200619 doi:http://dx.doi.org/10.2119/molmed.2009.00123
  6. ↑ Crichlow GV, Cheng KF, Dabideen D, Ochani M, Aljabari B, Pavlov VA, Miller EJ, Lolis E, Al-Abed Y. Alternative chemical modifications reverse the binding orientation of a pharmacophore scaffold in the active site of macrophage migration inhibitory factor. J Biol Chem. 2007 Aug 10;282(32):23089-95. Epub 2007 May 25. PMID:17526494 doi:http://dx.doi.org/10.1074/jbc.M701825200

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Michal Harel, Alexander Berchansky

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