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| | <StructureSection load='1h8a' size='340' side='right'caption='[[1h8a]], [[Resolution|resolution]] 2.23Å' scene=''> | | <StructureSection load='1h8a' size='340' side='right'caption='[[1h8a]], [[Resolution|resolution]] 2.23Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1h8a]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Amv Amv] and [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H8A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H8A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1h8a]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Avian_myeloblastosis_virus Avian myeloblastosis virus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H8A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H8A FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1h88|1h88]], [[1h89|1h89]], [[1hjb|1hjb]]</div></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]] 2.23Å</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=1h8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h8a OCA], [https://pdbe.org/1h8a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h8a RCSB], [https://www.ebi.ac.uk/pdbsum/1h8a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h8a 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=1h8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h8a OCA], [https://pdbe.org/1h8a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h8a RCSB], [https://www.ebi.ac.uk/pdbsum/1h8a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h8a ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/CEBPB_HUMAN CEBPB_HUMAN]] Important transcriptional activator in the regulation of genes involved in immune and inflammatory responses. Specifically binds to an IL-1 response element in the IL-6 gene. NF-IL6 also binds to regulatory regions of several acute-phase and cytokines genes. It probably plays a role in the regulation of acute-phase reaction, inflammation and hemopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Functions in brown adipose tissue (BAT) differentiation (By similarity). Regulates the transcriptional induction of peroxisome proliferator-activated receptor gamma (PPARG).<ref>PMID:20829347</ref>
| + | [https://www.uniprot.org/uniprot/CEBPB_HUMAN CEBPB_HUMAN] Important transcriptional activator in the regulation of genes involved in immune and inflammatory responses. Specifically binds to an IL-1 response element in the IL-6 gene. NF-IL6 also binds to regulatory regions of several acute-phase and cytokines genes. It probably plays a role in the regulation of acute-phase reaction, inflammation and hemopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Functions in brown adipose tissue (BAT) differentiation (By similarity). Regulates the transcriptional induction of peroxisome proliferator-activated receptor gamma (PPARG).<ref>PMID:20829347</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Amv]] | |
| - | [[Category: Human]] | |
| - | [[Category: Large Structures]] | |
| - | [[Category: Ogata, K]] | |
| - | [[Category: Tahirov, T H]] | |
| | [[Category: Avian myeloblastosis virus]] | | [[Category: Avian myeloblastosis virus]] |
| - | [[Category: Bzip]] | + | [[Category: Homo sapiens]] |
| - | [[Category: C-myb]] | + | [[Category: Large Structures]] |
| - | [[Category: C/ebp]] | + | [[Category: Ogata K]] |
| - | [[Category: Protein-dna complex]] | + | [[Category: Tahirov TH]] |
| - | [[Category: Transcription regulation]]
| + | |
| - | [[Category: Transcription-dna complex]]
| + | |
| - | [[Category: Transcription/dna]]
| + | |
| - | [[Category: Transforming protein]]
| + | |
| - | [[Category: V-myb]]
| + | |
| Structural highlights
Function
CEBPB_HUMAN Important transcriptional activator in the regulation of genes involved in immune and inflammatory responses. Specifically binds to an IL-1 response element in the IL-6 gene. NF-IL6 also binds to regulatory regions of several acute-phase and cytokines genes. It probably plays a role in the regulation of acute-phase reaction, inflammation and hemopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Functions in brown adipose tissue (BAT) differentiation (By similarity). Regulates the transcriptional induction of peroxisome proliferator-activated receptor gamma (PPARG).[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
c-Myb, but not avian myeloblastosis virus (AMV) v-Myb, cooperates with C/EBP beta to regulate transcription of myeloid-specific genes. To assess the structural basis for that difference, we determined the crystal structures of complexes comprised of the c-Myb or AMV v-Myb DNA-binding domain (DBD), the C/EBP beta DBD, and a promoter DNA fragment. Within the c-Myb complex, a DNA-bound C/EBP beta interacts with R2 of c-Myb bound to a different DNA fragment; point mutations in v-Myb R2 eliminate such interaction within the v-Myb complex. GST pull-down assays, luciferase trans-activation assays, and atomic force microscopy confirmed that the interaction of c-Myb and C/EBP beta observed in crystal mimics their long range interaction on the promoter, which is accompanied by intervening DNA looping.
Mechanism of c-Myb-C/EBP beta cooperation from separated sites on a promoter.,Tahirov TH, Sato K, Ichikawa-Iwata E, Sasaki M, Inoue-Bungo T, Shiina M, Kimura K, Takata S, Fujikawa A, Morii H, Kumasaka T, Yamamoto M, Ishii S, Ogata K Cell. 2002 Jan 11;108(1):57-70. PMID:11792321[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Park SH, Choi HJ, Yang H, Do KH, Kim J, Lee DW, Moon Y. Endoplasmic reticulum stress-activated C/EBP homologous protein enhances nuclear factor-kappaB signals via repression of peroxisome proliferator-activated receptor gamma. J Biol Chem. 2010 Nov 12;285(46):35330-9. doi: 10.1074/jbc.M110.136259. Epub 2010, Sep 9. PMID:20829347 doi:10.1074/jbc.M110.136259
- ↑ Tahirov TH, Sato K, Ichikawa-Iwata E, Sasaki M, Inoue-Bungo T, Shiina M, Kimura K, Takata S, Fujikawa A, Morii H, Kumasaka T, Yamamoto M, Ishii S, Ogata K. Mechanism of c-Myb-C/EBP beta cooperation from separated sites on a promoter. Cell. 2002 Jan 11;108(1):57-70. PMID:11792321
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