1fos: Difference between revisions

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New page: left|200px<br /> <applet load="1fos" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fos, resolution 3.050Å" /> '''TWO HUMAN C-FOS:C-...
 
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[[Image:1fos.gif|left|200px]]<br />
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'''TWO HUMAN C-FOS:C-JUN:DNA COMPLEXES'''<br />


==Overview==
==TWO HUMAN C-FOS:C-JUN:DNA COMPLEXES==
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.
<StructureSection load='1fos' size='340' side='right'caption='[[1fos]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
</table>
== Function ==
[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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fo/1fos_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1FOS 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=1FOS OCA].
*[[C-JUN|C-JUN]]
 
== References ==
==Reference==
<references/>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=7816143 7816143]
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Glover, J.N.M.]]
[[Category: Glover JNM]]
[[Category: Harrison, S.C.]]
[[Category: Harrison SC]]
[[Category: coiled-coil]]
[[Category: dna-binding protein]]
[[Category: heterodimer]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:55:49 2007''

Latest revision as of 10:17, 7 February 2024

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

Structural highlights

1fos is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.05Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Okazaki K, Sagata N. The Mos/MAP kinase pathway stabilizes c-Fos by phosphorylation and augments its transforming activity in NIH 3T3 cells. EMBO J. 1995 Oct 16;14(20):5048-59. PMID:7588633
  2. ↑ Zhang Y, Feng XH, Derynck R. Smad3 and Smad4 cooperate with c-Jun/c-Fos to mediate TGF-beta-induced transcription. Nature. 1998 Aug 27;394(6696):909-13. PMID:9732876 doi:10.1038/29814
  3. ↑ Bossis G, Malnou CE, Farras R, Andermarcher E, Hipskind R, Rodriguez M, Schmidt D, Muller S, Jariel-Encontre I, Piechaczyk M. Down-regulation of c-Fos/c-Jun AP-1 dimer activity by sumoylation. Mol Cell Biol. 2005 Aug;25(16):6964-79. PMID:16055710 doi:http://dx.doi.org/10.1128/MCB.25.16.6964-6979.2005

1fos, resolution 3.05Å

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