1fim: Difference between revisions
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==MACROPHAGE MIGRATION INHIBITORY FACTOR== | ==MACROPHAGE MIGRATION INHIBITORY FACTOR== | ||
<StructureSection load='1fim' size='340' side='right' caption='[[1fim]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1fim' size='340' side='right'caption='[[1fim]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1fim]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1fim]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FIM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FIM FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fim FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fim OCA], [https://pdbe.org/1fim PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fim RCSB], [https://www.ebi.ac.uk/pdbsum/1fim PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fim ProSAT]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/MIF_RAT MIF_RAT] 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 (By similarity). | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fi/1fim_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fi/1fim_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fim ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1fim" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Macrophage inhibitory factor|Macrophage inhibitory factor]] | *[[Macrophage inhibitory factor 3D structures|Macrophage inhibitory factor 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Nakagawa | [[Category: Nakagawa A]] | ||
[[Category: Sugimoto | [[Category: Sugimoto H]] | ||
[[Category: Suzuki | [[Category: Suzuki M]] | ||
[[Category: Tanaka | [[Category: Tanaka I]] | ||
Latest revision as of 12:38, 21 December 2022
MACROPHAGE MIGRATION INHIBITORY FACTORMACROPHAGE MIGRATION INHIBITORY FACTOR
Structural highlights
FunctionMIF_RAT 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 (By similarity). 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 PubMedThe tertiary structure of the macrophage migration inhibitory factor (MIF) from rat liver (12,300 Mr) is presented at 2.2 A resolution. Each monomer consists of two beta/alpha/beta motifs aligned in quasi two-fold symmetry, comprising a domain consisting of a four-stranded mixed beta-sheet and two antiparallel alpha-helices. The protein exists as a trimer in the crystal. An extra beta-strand that is almost perpendicular to the other beta-strands joins to the beta-sheet of the neighbouring monomer in the trimer. Unexpected similarities were detected between MIF and two kinds of isomerase. Crystal structure of the macrophage migration inhibitory factor from rat liver.,Suzuki M, Sugimoto H, Nakagawa A, Tanaka I, Nishihira J, Sakai M Nat Struct Biol. 1996 Mar;3(3):259-66. PMID:8605628[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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