1fos
From Proteopedia
(New page: 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 /> | + | [[Image:1fos.gif|left|200px]]<br /><applet load="1fos" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1fos" size=" | + | |
caption="1fos, resolution 3.050Å" /> | caption="1fos, resolution 3.050Å" /> | ||
'''TWO HUMAN C-FOS:C-JUN:DNA COMPLEXES'''<br /> | '''TWO HUMAN C-FOS:C-JUN:DNA COMPLEXES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Fos and Jun families of eukaryotic transcription factors | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 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:// | + | 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Glover, J | + | [[Category: Glover, J N.M.]] |
| - | [[Category: Harrison, S | + | [[Category: Harrison, S C.]] |
[[Category: coiled-coil]] | [[Category: coiled-coil]] | ||
[[Category: dna-binding protein]] | [[Category: dna-binding protein]] | ||
[[Category: heterodimer]] | [[Category: heterodimer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:54 2008'' |
Revision as of 10:40, 21 February 2008
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TWO HUMAN C-FOS:C-JUN:DNA COMPLEXES
Overview
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.
About this Structure
1FOS is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
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