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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<applet load="1fos" size="450" color="white" frame="true" align="right" spinBox="true"  
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'''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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FOS OCA].  
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.N.M.]]
[[Category: Glover, J N.M.]]
[[Category: Harrison, S.C.]]
[[Category: Harrison, S C.]]
[[Category: coiled-coil]]
[[Category: coiled-coil]]
[[Category: dna-binding protein]]
[[Category: dna-binding protein]]
[[Category: heterodimer]]
[[Category: heterodimer]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:54 2008''

Revision as of 13:40, 21 February 2008

File:1fos.gif


1fos, resolution 3.050Å

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

OverviewOverview

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 StructureAbout this Structure

1FOS is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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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