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| | <StructureSection load='4at9' size='340' side='right'caption='[[4at9]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='4at9' size='340' side='right'caption='[[4at9]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4at9]] is a 2 chain structure with sequence from [https://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=4AT9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AT9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4at9]] is a 2 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=4AT9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AT9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=UTP:URIDINE+5-TRIPHOSPHATE'>UTP</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]] 2.803Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4at7|4at7]], [[4at8|4at8]], [[4atb|4atb]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=UTP:URIDINE+5-TRIPHOSPHATE'>UTP</scene></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=4at9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4at9 OCA], [https://pdbe.org/4at9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4at9 RCSB], [https://www.ebi.ac.uk/pdbsum/4at9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4at9 ProSAT]</span></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=4at9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4at9 OCA], [https://pdbe.org/4at9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4at9 RCSB], [https://www.ebi.ac.uk/pdbsum/4at9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4at9 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/ILF2_MOUSE ILF2_MOUSE]] Appears to function predominantly as a heterodimeric complex with ILF3. This complex may regulate transcription of the IL2 gene during T-cell activation. It can also promote the formation of stable DNA-dependent protein kinase holoenzyme complexes on DNA (By similarity).<ref>PMID:10574923</ref> [[https://www.uniprot.org/uniprot/ILF3_MOUSE ILF3_MOUSE]] May facilitate double-stranded RNA-regulated gene expression at the level of post-transcription. Can act as a translation inhibitory protein which binds to coding sequences of acid beta-glucosidase (GCase) and other mRNAs and functions at the initiation phase of GCase mRNA translation, probably by inhibiting its binding to polysomes. Can regulate protein arginine N-methyltransferase 1 activity. Can promote the formation of stable DNA-dependent protein kinase holoenzyme complexes on DNA (By similarity).
| + | [https://www.uniprot.org/uniprot/ILF2_MOUSE ILF2_MOUSE] Appears to function predominantly as a heterodimeric complex with ILF3. This complex may regulate transcription of the IL2 gene during T-cell activation. It can also promote the formation of stable DNA-dependent protein kinase holoenzyme complexes on DNA (By similarity).<ref>PMID:10574923</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: Cook, A G]] | + | [[Category: Cook AG]] |
| - | [[Category: Wolkowicz, U M]] | + | [[Category: Wolkowicz UM]] |
| - | [[Category: Drpb76]]
| + | |
| - | [[Category: Ilf2]]
| + | |
| - | [[Category: Ilf3]]
| + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Nfar]]
| + | |
| - | [[Category: Template-free nucleotidyltransferase fold]]
| + | |
| Structural highlights
Function
ILF2_MOUSE Appears to function predominantly as a heterodimeric complex with ILF3. This complex may regulate transcription of the IL2 gene during T-cell activation. It can also promote the formation of stable DNA-dependent protein kinase holoenzyme complexes on DNA (By similarity).[1]
Publication Abstract from PubMed
Nuclear factors NF90 and NF45 form a complex involved in a variety of cellular processes and are thought to affect gene expression both at the transcriptional and translational level. In addition, this complex affects the replication of several viruses through direct interactions with viral RNA. NF90 and NF45 dimerize through their common 'DZF' domain (domain associated with zinc fingers). NF90 has additional double-stranded RNA-binding domains that likely mediate its association with target RNAs. We present the crystal structure of the NF90/NF45 dimerization complex at 1.9-A resolution. The DZF domain shows structural similarity to the template-free nucleotidyltransferase family of RNA modifying enzymes. However, both NF90 and NF45 have lost critical catalytic residues during evolution and are therefore not functional enzymes. Residues on NF90 that make up its interface with NF45 are conserved in two related proteins, spermatid perinuclear RNA-binding protein (SPNR) and zinc-finger RNA-binding protein (Zfr). Using a co-immunoprecipitation assay and site-specific mutants, we demonstrate that NF45 is also able to recognize SPNR and Zfr through the same binding interface, revealing that NF45 is able to form a variety of cellular complexes with other DZF-domain proteins.
NF45 dimerizes with NF90, Zfr and SPNR via a conserved domain that has a nucleotidyltransferase fold.,Wolkowicz UM, Cook AG Nucleic Acids Res. 2012 Oct 1;40(18):9356-68. doi: 10.1093/nar/gks696. Epub 2012 , Jul 24. PMID:22833610[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Satoh M, Shaheen VM, Kao PN, Okano T, Shaw M, Yoshida H, Richards HB, Reeves WH. Autoantibodies define a family of proteins with conserved double-stranded RNA-binding domains as well as DNA binding activity. J Biol Chem. 1999 Dec 3;274(49):34598-604. PMID:10574923
- ↑ Wolkowicz UM, Cook AG. NF45 dimerizes with NF90, Zfr and SPNR via a conserved domain that has a nucleotidyltransferase fold. Nucleic Acids Res. 2012 Oct 1;40(18):9356-68. doi: 10.1093/nar/gks696. Epub 2012 , Jul 24. PMID:22833610 doi:http://dx.doi.org/10.1093/nar/gks696
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