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1fos

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[[Image:1fos.gif|left|200px]]
 
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==TWO HUMAN C-FOS:C-JUN:DNA COMPLEXES==
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The line below this paragraph, containing "STRUCTURE_1fos", creates the "Structure Box" on the page.
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<StructureSection load='1fos' size='340' side='right'caption='[[1fos]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1fos]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FOS FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.05&#8491;</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=1fos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fos OCA], [https://pdbe.org/1fos PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fos RCSB], [https://www.ebi.ac.uk/pdbsum/1fos PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fos ProSAT]</span></td></tr>
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{{STRUCTURE_1fos| PDB=1fos | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FOS_HUMAN FOS_HUMAN] Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. In the heterodimer, FOS and JUN/AP-1 basic regions each seems to interact with symmetrical DNA half sites. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling. Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation.<ref>PMID:7588633</ref> <ref>PMID:9732876</ref> <ref>PMID:16055710</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/fo/1fos_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=1fos ConSurf].
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<div style="clear:both"></div>
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'''TWO HUMAN C-FOS:C-JUN:DNA COMPLEXES'''
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==See Also==
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*[[C-JUN|C-JUN]]
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== References ==
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==Overview==
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<references/>
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The Fos and Jun families of eukaryotic transcription factors heterodimerize to form complexes capable of binding 5'-TGAGTCA-3' DNA elements. We have determined the X-ray crystal structure of a heterodimer of the bZIP regions of c-Fos and c-Jun bound to DNA. Both subunits form continuous alpha-helices. The carboxy-terminal regions form an asymmetric coiled-coil, and the amino-terminal regions make base-specific contacts with DNA in the major groove. Comparison of the two crystallographically distinct protein-DNA complexes show that the coiled-coil is flexibly joined to the basic regions and that the Fos-Jun heterodimer does not recognize the asymmetric 5'-TGAGTCA-3' recognition element in a unique orientation. There is an extensive network of electrostatic interactions between subunits within the coiled-coil, consistent with proposals that these interactions determine preferential formation of the heterodimer over either of the homodimers.
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__TOC__
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</StructureSection>
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==About this Structure==
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1FOS is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOS OCA].
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==Reference==
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Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA., Glover JN, Harrison SC, Nature. 1995 Jan 19;373(6511):257-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7816143 7816143]
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[[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: Glover, J N.M.]]
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[[Category: Glover JNM]]
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[[Category: Harrison, S C.]]
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[[Category: Harrison SC]]
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[[Category: Coiled-coil]]
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[[Category: Dna-binding protein]]
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[[Category: Heterodimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:35:14 2008''
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Current revision

TWO HUMAN C-FOS:C-JUN:DNA COMPLEXES

PDB ID 1fos

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