1o4x

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(New page: 200px<br /> <applet load="1o4x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o4x" /> '''TERNARY COMPLEX OF THE DNA BINDING DOMAINS ...)
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[[Image:1o4x.gif|left|200px]]<br />
 
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'''TERNARY COMPLEX OF THE DNA BINDING DOMAINS OF THE OCT1 AND SOX2 TRANSCRIPTION FACTORS WITH A 19MER OLIGONUCLEOTIDE FROM THE HOXB1 REGULATORY ELEMENT'''<br />
 
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==Overview==
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==TERNARY COMPLEX OF THE DNA BINDING DOMAINS OF THE OCT1 AND SOX2 TRANSCRIPTION FACTORS WITH A 19MER OLIGONUCLEOTIDE FROM THE HOXB1 REGULATORY ELEMENT==
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The Oct and Sox transcription factors control many different aspects of, neural development and embryogenesis, often binding to adjacent sites on, DNA, and interacting with one another through their DNA binding domains to, regulate transcription synergistically. Oct proteins contain two DNA, binding domains (POUS and POUHD) connected by a flexible linker, which, interact with DNA in a bipartite manner. Residual dipolar coupling, measurements on the binary Oct1.DNA complex reveal that the two domains, are characterized by distinct alignment tensors in both phage pf1 and, polyethylene glycol/hexanol liquid crystalline media. We show that this, difference is due to a fast microscopic dissociation/association process, involving alternative binding modes for the weaker binding POUS domain in, the binary complex. Upon binding of Sox2 to an adjacent site in the Hoxb1, regulatory element, all components of the ternary Oct1.Sox2.DNA complex, share a single alignment tensor. Thus ternary complex formation increases, the site-specific affinity of Oct1 for DNA by effectively locking the POUS, domain in a single orientation on the DNA. The solution NMR structure of, the ternary 42 kDa Oct1.Sox2.Hoxb1-DNA complex, determined by novel, procedures based on orientational restraints from dipolar couplings and, conjoined rigid body/torsion angle dynamics, reveals that Sox2 and POUS, interact through a predominantly hydrophobic interface, surrounded by a, ring of electrostatic interactions. These observations suggest a mechanism, of combinatorial control involving direct protein-protein interactions on, the DNA whereby Oct1 in conjunction with a co-interacting transcription, factor provide cell-specific transcription regulation.
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<StructureSection load='1o4x' size='340' side='right'caption='[[1o4x]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1o4x]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The April 2009 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Oct and Sox Transcription Factors'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2009_4 10.2210/rcsb_pdb/mom_2009_4]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O4X FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1o4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o4x OCA], [https://pdbe.org/1o4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o4x RCSB], [https://www.ebi.ac.uk/pdbsum/1o4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o4x ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PO2F1_HUMAN PO2F1_HUMAN] Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') and activates the promoters of the genes for some small nuclear RNAs (snRNA) and of genes such as those for histone H2B and immunoglobulins. Modulates transcription transactivation by NR3C1, AR and PGR (By similarity). In case of human herpes simplex virus (HSV) infection, POU2F1 forms a multiprotein-DNA complex with the viral transactivator protein VP16 and HCFC1 thereby enabling the transcription of the viral immediate early genes.<ref>PMID:1684878</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o4/1o4x_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1o4x ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The Oct and Sox transcription factors control many different aspects of neural development and embryogenesis, often binding to adjacent sites on DNA, and interacting with one another through their DNA binding domains to regulate transcription synergistically. Oct proteins contain two DNA binding domains (POUS and POUHD) connected by a flexible linker, which interact with DNA in a bipartite manner. Residual dipolar coupling measurements on the binary Oct1.DNA complex reveal that the two domains are characterized by distinct alignment tensors in both phage pf1 and polyethylene glycol/hexanol liquid crystalline media. We show that this difference is due to a fast microscopic dissociation/association process involving alternative binding modes for the weaker binding POUS domain in the binary complex. Upon binding of Sox2 to an adjacent site in the Hoxb1 regulatory element, all components of the ternary Oct1.Sox2.DNA complex share a single alignment tensor. Thus ternary complex formation increases the site-specific affinity of Oct1 for DNA by effectively locking the POUS domain in a single orientation on the DNA. The solution NMR structure of the ternary 42 kDa Oct1.Sox2.Hoxb1-DNA complex, determined by novel procedures based on orientational restraints from dipolar couplings and conjoined rigid body/torsion angle dynamics, reveals that Sox2 and POUS interact through a predominantly hydrophobic interface, surrounded by a ring of electrostatic interactions. These observations suggest a mechanism of combinatorial control involving direct protein-protein interactions on the DNA whereby Oct1 in conjunction with a co-interacting transcription factor provide cell-specific transcription regulation.
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==Disease==
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Molecular basis for synergistic transcriptional activation by Oct1 and Sox2 revealed from the solution structure of the 42-kDa Oct1.Sox2.Hoxb1-DNA ternary transcription factor complex.,Williams DC Jr, Cai M, Clore GM J Biol Chem. 2004 Jan 9;279(2):1449-57. Epub 2003 Oct 14. PMID:14559893<ref>PMID:14559893</ref>
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Known diseases associated with this structure: Microphthalmia, syndromic 3 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=184429 184429]], Optic nerve hypoplasia and abnormalities of the central nervous system OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=184429 184429]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1O4X is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O4X OCA].
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</div>
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<div class="pdbe-citations 1o4x" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Molecular basis for synergistic transcriptional activation by Oct1 and Sox2 revealed from the solution structure of the 42-kDa Oct1.Sox2.Hoxb1-DNA ternary transcription factor complex., Williams DC Jr, Cai M, Clore GM, J Biol Chem. 2004 Jan 9;279(2):1449-57. Epub 2003 Oct 14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14559893 14559893]
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*[[OCT4 and SOX2 transcription factors|OCT4 and SOX2 transcription factors]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Clore, G.M.]]
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[[Category: Oct and Sox Transcription Factors]]
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[[Category: Williams, D.C.]]
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[[Category: RCSB PDB Molecule of the Month]]
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[[Category: dna]]
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[[Category: Clore GM]]
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[[Category: hmg-box]]
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[[Category: Williams DC]]
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[[Category: oct1]]
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[[Category: pou]]
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[[Category: pouhd]]
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[[Category: pous]]
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[[Category: protein-dna complex]]
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[[Category: sox2]]
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[[Category: transcription factors]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:29:38 2007''
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Current revision

TERNARY COMPLEX OF THE DNA BINDING DOMAINS OF THE OCT1 AND SOX2 TRANSCRIPTION FACTORS WITH A 19MER OLIGONUCLEOTIDE FROM THE HOXB1 REGULATORY ELEMENT

PDB ID 1o4x

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