1gu5: Difference between revisions
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<StructureSection load='1gu5' size='340' side='right' caption='[[1gu5]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1gu5' size='340' side='right' caption='[[1gu5]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1gu5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1gu5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GU5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GU5 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gtw|1gtw]], [[1gu4|1gu4]], [[1h88|1h88]], [[1h89|1h89]], [[1h8a|1h8a]], [[1hjb|1hjb]], [[1io4|1io4]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gtw|1gtw]], [[1gu4|1gu4]], [[1h88|1h88]], [[1h89|1h89]], [[1h8a|1h8a]], [[1hjb|1hjb]], [[1io4|1io4]]</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=1gu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gu5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gu5 RCSB], [http://www.ebi.ac.uk/pdbsum/1gu5 PDBsum]</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=1gu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gu5 OCA], [http://pdbe.org/1gu5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gu5 RCSB], [http://www.ebi.ac.uk/pdbsum/1gu5 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1gu5" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Human]] | ||
[[Category: Ogata, K]] | [[Category: Ogata, K]] | ||
[[Category: Tahirov, T H]] | [[Category: Tahirov, T H]] | ||
Revision as of 20:17, 11 September 2015
CRYSTAL STRUCTURE OF C/EBPBETA BZIP DIMERIC BOUND TO A DNA FRAGMENT FROM THE MIM-1 PROMOTERCRYSTAL STRUCTURE OF C/EBPBETA BZIP DIMERIC BOUND TO A DNA FRAGMENT FROM THE MIM-1 PROMOTER
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 PubMedc-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
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