1fos
From Proteopedia
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| - | [[Image:1fos.gif|left|200px]] | + | [[Image:1fos.gif|left|200px]] |
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| - | '''TWO HUMAN C-FOS:C-JUN:DNA COMPLEXES''' | + | {{Structure |
| + | |PDB= 1fos |SIZE=350|CAPTION= <scene name='initialview01'>1fos</scene>, resolution 3.050Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''TWO HUMAN C-FOS:C-JUN:DNA COMPLEXES''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FOS is a [ | + | 1FOS is a [[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== | ||
| - | 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:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/7816143 7816143] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: heterodimer]] | [[Category: heterodimer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:11:56 2008'' |
Revision as of 09:11, 20 March 2008
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| , resolution 3.050Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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