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=''> | ||
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<table><tr><td colspan='2'>[[1fim]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FIM FirstGlance]. <br> | <table><tr><td colspan='2'>[[1fim]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FIM FirstGlance]. <br> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fim FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fim OCA], [http://pdbe.org/1fim PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fim RCSB], [http://www.ebi.ac.uk/pdbsum/1fim PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fim FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fim OCA], [http://pdbe.org/1fim PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fim RCSB], [http://www.ebi.ac.uk/pdbsum/1fim PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fim ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 1fim" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1fim" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:34, 29 November 2017
MACROPHAGE MIGRATION INHIBITORY FACTORMACROPHAGE MIGRATION INHIBITORY FACTOR
Structural highlights
Function[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 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. References |
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