1gu5

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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 Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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.

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[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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
  2. Tahirov TH, Inoue-Bungo T, Sasaki M, Shiina M, Kimura K, Sato K, Kumasaka T, Yamamoto M, Kamiya N, Ogata K. 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. Acta Crystallogr D Biol Crystallogr. 2001 Jun;57(Pt 6):850-3. Epub 2001, May 25. PMID:11375505

1gu5, resolution 2.10Å

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