1gtw: Difference between revisions
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==crystal structure of C/EBPbeta bZip homodimer bound to a DNA fragment from the tom-1A promoter== | ==crystal structure of C/EBPbeta bZip homodimer bound to a DNA fragment from the tom-1A promoter== | ||
<StructureSection load='1gtw' size='340' side='right' caption='[[1gtw]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='1gtw' size='340' side='right' caption='[[1gtw]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
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<table><tr><td colspan='2'>[[1gtw]] 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=1GTW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GTW FirstGlance]. <br> | <table><tr><td colspan='2'>[[1gtw]] 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=1GTW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GTW FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gu4|1gu4]], [[1gu5|1gu5]], [[1h88|1h88]], [[1h89|1h89]], [[1h8a|1h8a]], [[1hjb|1hjb]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gu4|1gu4]], [[1gu5|1gu5]], [[1h88|1h88]], [[1h89|1h89]], [[1h8a|1h8a]], [[1hjb|1hjb]]</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=1gtw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gtw OCA], [http://pdbe.org/1gtw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gtw RCSB], [http://www.ebi.ac.uk/pdbsum/1gtw 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=1gtw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gtw OCA], [http://pdbe.org/1gtw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gtw RCSB], [http://www.ebi.ac.uk/pdbsum/1gtw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gtw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gt/1gtw_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gt/1gtw_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 09:39, 3 January 2018
crystal structure of C/EBPbeta bZip homodimer bound to a DNA fragment from the tom-1A promotercrystal structure of C/EBPbeta bZip homodimer bound to a DNA fragment from the tom-1A 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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