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| | ==Crystal structure of Max-E47== | | ==Crystal structure of Max-E47== |
| - | <StructureSection load='3u5v' size='340' side='right' caption='[[3u5v]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='3u5v' size='340' side='right'caption='[[3u5v]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3u5v]] is a 1 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=3U5V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U5V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3u5v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U5V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U5V FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Max, Myn, BHLHB21, E2A, ITF1, TCF3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Max, Myn, BHLHB21, E2A, ITF1, TCF3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3u5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u5v OCA], [http://pdbe.org/3u5v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3u5v RCSB], [http://www.ebi.ac.uk/pdbsum/3u5v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3u5v 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=3u5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u5v OCA], [https://pdbe.org/3u5v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u5v RCSB], [https://www.ebi.ac.uk/pdbsum/3u5v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u5v ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MAX_MOUSE MAX_MOUSE]] Transcription regulator. Forms a sequence-specific DNA-binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC-MAX complex is a transcriptional activator, whereas the MAD-MAX complex is a repressor. CpG methylation of the recognition site greatly inhibits DNA binding, suggesting that DNA methylation may regulate the MYC/MAX complex in vivo. May repress transcription via the recruitment of a chromatin remodeling complex containing H3 'Lys-9' histone methyltransferase activity. | + | [[https://www.uniprot.org/uniprot/MAX_MOUSE MAX_MOUSE]] Transcription regulator. Forms a sequence-specific DNA-binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC-MAX complex is a transcriptional activator, whereas the MAD-MAX complex is a repressor. CpG methylation of the recognition site greatly inhibits DNA binding, suggesting that DNA methylation may regulate the MYC/MAX complex in vivo. May repress transcription via the recruitment of a chromatin remodeling complex containing H3 'Lys-9' histone methyltransferase activity. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Human]] | | [[Category: Human]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Ahmadpour, F]] | | [[Category: Ahmadpour, F]] |
| | [[Category: Gloyd, M]] | | [[Category: Gloyd, M]] |
| Structural highlights
3u5v is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | |
| Gene: | Max, Myn, BHLHB21, E2A, ITF1, TCF3 (HUMAN) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[MAX_MOUSE] Transcription regulator. Forms a sequence-specific DNA-binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC-MAX complex is a transcriptional activator, whereas the MAD-MAX complex is a repressor. CpG methylation of the recognition site greatly inhibits DNA binding, suggesting that DNA methylation may regulate the MYC/MAX complex in vivo. May repress transcription via the recruitment of a chromatin remodeling complex containing H3 'Lys-9' histone methyltransferase activity.
Publication Abstract from PubMed
Max-E47 is a protein chimera generated from the fusion of the DNA-binding basic region of Max and the dimerization region of E47, both members of the basic region/helix-loop-helix (bHLH) superfamily of transcription factors. Like native Max, Max-E47 binds with high affinity and specificity to the E-box site, 5'-CACGTG, both in vivo and in vitro. We have determined the crystal structure of Max-E47 at 1.7 A resolution, and found that it associates to form a well-structured dimer even in the absence of its cognate DNA. Analytical ultracentrifugation confirms that Max-E47 is dimeric even at low micromolar concentrations, indicating that the Max-E47 dimer is stable in the absence of DNA. Circular dichroism analysis demonstrates that both non-specific DNA and the E-box site induce similar levels of helical secondary structure in Max-E47. These results suggest that Max-E47 may bind to the E-box following the two-step mechanism proposed for other bHLH proteins. In this mechanism, a rapid step where protein binds to DNA without sequence specificity is followed by a slow step where specific protein:DNA interactions are fine-tuned, leading to sequence-specific recognition. Collectively, these results show that the designed Max-E47 protein chimera behaves both structurally and functionally like its native counterparts.
Crystal structure of the minimalist max-e47 protein chimera.,Ahmadpour F, Ghirlando R, De Jong AT, Gloyd M, Shin JA, Guarne A PLoS One. 2012;7(2):e32136. Epub 2012 Feb 28. PMID:22389683[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ahmadpour F, Ghirlando R, De Jong AT, Gloyd M, Shin JA, Guarne A. Crystal structure of the minimalist max-e47 protein chimera. PLoS One. 2012;7(2):e32136. Epub 2012 Feb 28. PMID:22389683 doi:10.1371/journal.pone.0032136
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