1fos: Difference between revisions
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</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=1fos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fos OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fos RCSB], [http://www.ebi.ac.uk/pdbsum/1fos PDBsum]</span></td></tr> | </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=1fos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fos OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fos RCSB], [http://www.ebi.ac.uk/pdbsum/1fos PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 01:40, 26 December 2014
TWO HUMAN C-FOS:C-JUN:DNA COMPLEXESTWO HUMAN C-FOS:C-JUN:DNA COMPLEXES
Structural highlights
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. Publication Abstract from PubMedThe 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. 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:7816143[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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