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| | <StructureSection load='6oe9' size='340' side='right'caption='[[6oe9]], [[Resolution|resolution]] 1.94Å' scene=''> | | <StructureSection load='6oe9' size='340' side='right'caption='[[6oe9]], [[Resolution|resolution]] 1.94Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6oe9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OE9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OE9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6oe9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OE9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OE9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.94Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4l5q|4l5q]], [[4l5r|4l5r]], [[4l5s|4l5s]], [[2oq0|2oq0]], [[5yzp|5yzp]], [[5z7d|5z7d]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ifi204 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=6oe9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oe9 OCA], [https://pdbe.org/6oe9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oe9 RCSB], [https://www.ebi.ac.uk/pdbsum/6oe9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oe9 ProSAT]</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=6oe9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oe9 OCA], [http://pdbe.org/6oe9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oe9 RCSB], [http://www.ebi.ac.uk/pdbsum/6oe9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oe9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/IFI4_MOUSE IFI4_MOUSE]] Inhibits the transcription of ribosomal RNA. May inhibit DNA binding by UBTF. Inhibits cell growth via p53/TP53 and RB1-dependent and independent pathways. Acts as a coactivator of RUNX2 during osteogenesis. May be involved in macrophage differentiation. Enables skeletal muscle and cardiac myocyte differentiation by sequestring Id proteins in the cytosol and promoting their ubiquitination and subsequent degradation.<ref>PMID:10329630</ref> <ref>PMID:11940648</ref> <ref>PMID:15557274</ref> <ref>PMID:16244109</ref> <ref>PMID:16458891</ref> <ref>PMID:16556595</ref> <ref>PMID:16556596</ref> | + | [https://www.uniprot.org/uniprot/IFI4_MOUSE IFI4_MOUSE] Inhibits the transcription of ribosomal RNA. May inhibit DNA binding by UBTF. Inhibits cell growth via p53/TP53 and RB1-dependent and independent pathways. Acts as a coactivator of RUNX2 during osteogenesis. May be involved in macrophage differentiation. Enables skeletal muscle and cardiac myocyte differentiation by sequestring Id proteins in the cytosol and promoting their ubiquitination and subsequent degradation.<ref>PMID:10329630</ref> <ref>PMID:11940648</ref> <ref>PMID:15557274</ref> <ref>PMID:16244109</ref> <ref>PMID:16458891</ref> <ref>PMID:16556595</ref> <ref>PMID:16556596</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Tian, Y]] | + | [[Category: Tian Y]] |
| - | [[Category: Yin, Q]] | + | [[Category: Yin Q]] |
| - | [[Category: Cytosolic protein]]
| + | |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Immune system]]
| + | |
| Structural highlights
Function
IFI4_MOUSE Inhibits the transcription of ribosomal RNA. May inhibit DNA binding by UBTF. Inhibits cell growth via p53/TP53 and RB1-dependent and independent pathways. Acts as a coactivator of RUNX2 during osteogenesis. May be involved in macrophage differentiation. Enables skeletal muscle and cardiac myocyte differentiation by sequestring Id proteins in the cytosol and promoting their ubiquitination and subsequent degradation.[1] [2] [3] [4] [5] [6] [7]
Publication Abstract from PubMed
Interferon-inducible protein 204 (p204) binds to microbial DNA to elicit inflammatory responses and induce interferon production. p204 also modulates cell proliferation and differentiation by regulating various transcription factors. The C-terminal HIN domains in p204 are believed to be responsible for DNA binding, but the binding mode is not fully understood. The DNA-binding affinity of the p204 HIN1 domain has been characterized and its crystal structure has been determined, providing insight into its interaction with DNA. Surface-charge distribution together with sequence alignment suggests that the p204 HIN domain uses its L12 and L45 loops for DNA binding.
Structural analysis of the HIN1 domain of interferon-inducible protein 204.,Tian Y, Yin Q Acta Crystallogr F Struct Biol Commun. 2019 Jun 1;75(Pt 6):455-460. doi:, 10.1107/S2053230X19007167. Epub 2019 Jun 10. PMID:31204693[8]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu CJ, Wang H, Lengyel P. The interferon-inducible nucleolar p204 protein binds the ribosomal RNA-specific UBF1 transcription factor and inhibits ribosomal RNA transcription. EMBO J. 1999 May 17;18(10):2845-54. PMID:10329630 doi:http://dx.doi.org/10.1093/emboj/18.10.2845
- ↑ Liu CJ, Ding B, Wang H, Lengyel P. The MyoD-inducible p204 protein overcomes the inhibition of myoblast differentiation by Id proteins. Mol Cell Biol. 2002 May;22(9):2893-905. PMID:11940648
- ↑ Liu CJ, Chang E, Yu J, Carlson CS, Prazak L, Yu XP, Ding B, Lengyel P, Di Cesare PE. The interferon-inducible p204 protein acts as a transcriptional coactivator of Cbfa1 and enhances osteoblast differentiation. J Biol Chem. 2005 Jan 28;280(4):2788-96. doi: 10.1074/jbc.M412604200. Epub 2004, Nov 19. PMID:15557274 doi:http://dx.doi.org/10.1074/jbc.M412604200
- ↑ Dauffy J, Mouchiroud G, Bourette RP. The interferon-inducible gene, Ifi204, is transcriptionally activated in response to M-CSF, and its expression favors macrophage differentiation in myeloid progenitor cells. J Leukoc Biol. 2006 Jan;79(1):173-83. Epub 2005 Oct 21. PMID:16244109 doi:http://dx.doi.org/jlb.0205083
- ↑ Asefa B, Dermott JM, Kaldis P, Stefanisko K, Garfinkel DJ, Keller JR. p205, a potential tumor suppressor, inhibits cell proliferation via multiple pathways of cell cycle regulation. FEBS Lett. 2006 Feb 20;580(5):1205-14. Epub 2006 Jan 20. PMID:16458891 doi:http://dx.doi.org/10.1016/j.febslet.2006.01.032
- ↑ Ding B, Liu CJ, Huang Y, Hickey RP, Yu J, Kong W, Lengyel P. p204 is required for the differentiation of P19 murine embryonal carcinoma cells to beating cardiac myocytes: its expression is activated by the cardiac Gata4, Nkx2.5, and Tbx5 proteins. J Biol Chem. 2006 May 26;281(21):14882-92. doi: 10.1074/jbc.M511747200. Epub 2006, Mar 22. PMID:16556595 doi:http://dx.doi.org/10.1074/jbc.M511747200
- ↑ Ding B, Liu CJ, Huang Y, Yu J, Kong W, Lengyel P. p204 protein overcomes the inhibition of the differentiation of P19 murine embryonal carcinoma cells to beating cardiac myocytes by Id proteins. J Biol Chem. 2006 May 26;281(21):14893-906. doi: 10.1074/jbc.M511748200. Epub, 2006 Mar 22. PMID:16556596 doi:http://dx.doi.org/10.1074/jbc.M511748200
- ↑ Tian Y, Yin Q. Structural analysis of the HIN1 domain of interferon-inducible protein 204. Acta Crystallogr F Struct Biol Commun. 2019 Jun 1;75(Pt 6):455-460. doi:, 10.1107/S2053230X19007167. Epub 2019 Jun 10. PMID:31204693 doi:http://dx.doi.org/10.1107/S2053230X19007167
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