6oe9
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of p204 HIN1 domain== | |
| + | <StructureSection load='6oe9' size='340' side='right'caption='[[6oe9]], [[Resolution|resolution]] 1.94Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6oe9]] is a 1 chain structure. 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> | ||
| + | </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> | ||
| + | <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='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> | ||
| + | == 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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:31204693</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6oe9" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Tian, Y]] | ||
| + | [[Category: Yin, Q]] | ||
| + | [[Category: Cytosolic protein]] | ||
| + | [[Category: Dna binding protein]] | ||
| + | [[Category: Immune system]] | ||
Revision as of 05:49, 10 July 2019
Crystal structure of p204 HIN1 domain
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