1gu5: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
Line 3: Line 3:
<StructureSection load='1gu5' size='340' side='right'caption='[[1gu5]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='1gu5' size='340' side='right'caption='[[1gu5]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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://proteopedia.org/fgij/fg.htm?mol=1GU5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1gu5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. 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 [https://proteopedia.org/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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gu5 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=1gu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gu5 OCA], [https://pdbe.org/1gu5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gu5 RCSB], [https://www.ebi.ac.uk/pdbsum/1gu5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gu5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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]]
Line 19: Line 19:
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gu5 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gu5 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Three types of protein-DNA complexes, AML1/Runx-1/CBFalpha(Runt)-CBFbeta-C/EBPbeta(bZip)-DNA (CBFalpha-beta-C/EBPbeta-DNA), AML1/Runx-1/CBFalpha(Runt)-C/EBPbeta(bZip)-DNA (CBFalpha-C/EBPbeta-DNA) and AML1/Runx-1/CBFalpha(Runt)-DNA (CBFalpha-DNA), were crystallized. The crystals were all orthorhombic and belonged to space groups C222(1), P2(1)2(1)2 and P2(1)2(1)2(1), respectively. The resolutions of CBFalpha-beta-C/EBPbeta-DNA and CBFalpha-C/EBPbeta-DNA crystals were both 3 A, while that of the CBFalpha-DNA crystal was 2.65 A. Complete data sets were collected for all of the native crystals, along with MAD and MIR data sets for CBFalpha-beta-C/EBPbeta-DNA. The heavy-atom site was determined using MAD data for a gold derivative of CBFalpha-beta-C/EBPbeta-DNA.
Crystallization and preliminary X-ray analyses of quaternary, ternary and binary protein-DNA complexes with involvement of AML1/Runx-1/CBFalpha Runt domain, CBFbeta and the C/EBPbeta bZip region.,Tahirov TH, Inoue-Bungo T, Sasaki M, Shiina M, Kimura K, Sato K, Kumasaka T, Yamamoto M, Kamiya N, Ogata K Acta Crystallogr D Biol Crystallogr. 2001 Jun;57(Pt 6):850-3. Epub 2001, May 25. PMID:11375505<ref>PMID:11375505</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1gu5" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ogata, K]]
[[Category: Synthetic construct]]
[[Category: Tahirov, T H]]
[[Category: Ogata K]]
[[Category: Bzip]]
[[Category: Tahirov TH]]
[[Category: C/ebp]]
[[Category: Protein-dna complex]]
[[Category: Transcription factor]]
[[Category: Transcription-dna complex]]
[[Category: Transcription/dna]]

Latest revision as of 15:06, 13 December 2023

Crystal structure of C/EBPBETA BZIP homodimer bound to a DNA fragment from the MIM-1 promoterCrystal structure of C/EBPBETA BZIP homodimer bound to a DNA fragment from the MIM-1 promoter

Structural highlights

1gu5 is a 4 chain structure with sequence from Homo sapiens and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

References

  1. ↑ 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

1gu5, resolution 2.10Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1gu5&oldid=3980681"