1fos
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(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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Revision as of 14:49, 12 November 2007
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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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