1fos: Difference between revisions
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[[Image: | ==TWO HUMAN C-FOS:C-JUN:DNA COMPLEXES== | ||
<StructureSection load='1fos' size='340' side='right' caption='[[1fos]], [[Resolution|resolution]] 3.05Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1fos]] is a 8 chain structure with sequence 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FOS FirstGlance]. <br> | |||
</td></tr><tr><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> | |||
== 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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:7816143</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[C-JUN|C-JUN]] | *[[C-JUN|C-JUN]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Glover, J N.M.]] | [[Category: Glover, J N.M.]] | ||
Revision as of 17:19, 28 September 2014
TWO HUMAN C-FOS:C-JUN:DNA COMPLEXESTWO HUMAN C-FOS:C-JUN:DNA COMPLEXES
Structural highlights
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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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