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| | ==SOLUTION STRUCTURE OF MYELOID PROGENITOR INHIBITORY FACTOR-1 (MPIF-1)== | | ==SOLUTION STRUCTURE OF MYELOID PROGENITOR INHIBITORY FACTOR-1 (MPIF-1)== |
| - | <StructureSection load='1g91' size='340' side='right' caption='[[1g91]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | + | <StructureSection load='1g91' size='340' side='right'caption='[[1g91]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1g91]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G91 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G91 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1g91]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G91 FirstGlance]. <br> |
| - | </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=1g91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g91 OCA], [http://pdbe.org/1g91 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g91 RCSB], [http://www.ebi.ac.uk/pdbsum/1g91 PDBsum]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 30 models</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=1g91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g91 OCA], [https://pdbe.org/1g91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g91 RCSB], [https://www.ebi.ac.uk/pdbsum/1g91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g91 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CCL23_HUMAN CCL23_HUMAN]] Shows chemotactic activity for monocytes, resting T-lymphocytes, and neutrophils, but not for activated lymphocytes. Inhibits proliferation of myeloid progenitor cells in colony formation assays. This protein can bind heparin. Binds CCR1. CCL23(19-99), CCL23(22-99), CCL23(27-99), CCL23(30-99) are more potent chemoattractants than the small-inducible cytokine A23.<ref>PMID:15905581</ref> | + | [https://www.uniprot.org/uniprot/CCL23_HUMAN CCL23_HUMAN] Shows chemotactic activity for monocytes, resting T-lymphocytes, and neutrophils, but not for activated lymphocytes. Inhibits proliferation of myeloid progenitor cells in colony formation assays. This protein can bind heparin. Binds CCR1. CCL23(19-99), CCL23(22-99), CCL23(27-99), CCL23(30-99) are more potent chemoattractants than the small-inducible cytokine A23.<ref>PMID:15905581</ref> |
| | == 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/g9/1g91_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g9/1g91_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Gentz, R]] | + | [[Category: Large Structures]] |
| - | [[Category: Li, Y]] | + | [[Category: Gentz R]] |
| - | [[Category: Rajarathnam, K]] | + | [[Category: Li Y]] |
| - | [[Category: Rohrer, T]] | + | [[Category: Rajarathnam K]] |
| - | [[Category: Ccl23]]
| + | [[Category: Rohrer T]] |
| - | [[Category: Chemokine]]
| + | |
| - | [[Category: Ckb8]]
| + | |
| - | [[Category: Cytokine]]
| + | |
| - | [[Category: Mpif-1]]
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| Structural highlights
Function
CCL23_HUMAN Shows chemotactic activity for monocytes, resting T-lymphocytes, and neutrophils, but not for activated lymphocytes. Inhibits proliferation of myeloid progenitor cells in colony formation assays. This protein can bind heparin. Binds CCR1. CCL23(19-99), CCL23(22-99), CCL23(27-99), CCL23(30-99) are more potent chemoattractants than the small-inducible cytokine A23.[1]
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 PubMed
MPIF-1, a CC chemokine, is a specific inhibitor of myeloid progenitor cells and is the most potent activator of monocytes. The solution structure of myeloid progenitor inhibitor factor-1 (MPIF-1) has been determined by NMR spectroscopy. The structure reveals that MPIF-1 is a monomer with a well defined core except for termini residues and adopts the chemokine fold of three beta-strands and an overlying alpha-helix. In addition to the four cysteines that characterize most chemokines, MPIF-1 has two additional cysteines that form a disulfide bond. The backbone dynamics indicate that the disulfide bonds and the adjacent residues that include the functionally important N-terminal and N-terminal loop residues show significant dynamics. MPIF-1 is a highly basic protein (pI >9), and the structure reveals distinct positively charged pockets that could be correlated to proteoglycan binding. MPIF-1 is processed from a longer proprotein at the N terminus and the latter is also functional though with reduced potency, and both proteins exist as monomers under a variety of solution conditions. MPIF-1 is therefore unique because longer proproteins of all other chemokines oligomerize in solution. The MPIF-1 structure should serve as a template for future functional studies that could lead to therapeutics for preventing chemotherapy-associated myelotoxicity.
Solution structure and dynamics of myeloid progenitor inhibitory factor-1 (MPIF-1), a novel monomeric CC chemokine.,Rajarathnam K, Li Y, Rohrer T, Gentz R J Biol Chem. 2001 Feb 16;276(7):4909-16. Epub 2000 Nov 1. PMID:11060285[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Berahovich RD, Miao Z, Wang Y, Premack B, Howard MC, Schall TJ. Proteolytic activation of alternative CCR1 ligands in inflammation. J Immunol. 2005 Jun 1;174(11):7341-51. PMID:15905581
- ↑ Rajarathnam K, Li Y, Rohrer T, Gentz R. Solution structure and dynamics of myeloid progenitor inhibitory factor-1 (MPIF-1), a novel monomeric CC chemokine. J Biol Chem. 2001 Feb 16;276(7):4909-16. Epub 2000 Nov 1. PMID:11060285 doi:10.1074/jbc.M005085200
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