C-JUN: Difference between revisions
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= C-JUN = | = C-JUN = | ||
<applet load='1Z82' size='200' frame='true' align='right' caption='1JUN' /> | <applet load='1Z82' size='200' frame='true' align='right' caption='1JUN' /> | ||
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The c-Jun protein is a member of transcription factors which consist of a basic region leucine zipper region <ref name="ref1"> PMID:8662824 </ref>. All these leucine zipper factors bind to DNA in one of two states: homo or heterodimers <ref name="ref1"/>.. In conjunction with the c-Fos protein these two proteins bind to specific regions of DNA strands. Together these two proteins form the c-fos/c-jun complex which help regulate cell growth and differentiation <ref name="ref1"/>. Regulation of the complex iteslf is done by interactions between the protein and DNA in addition to the protein-protein interactions between each of the leucine zipper domains <ref name="ref1"/>. | The c-Jun protein is a member of transcription factors which consist of a basic region leucine zipper region <ref name="ref1"> PMID:8662824 </ref>. All these leucine zipper factors bind to DNA in one of two states: homo or heterodimers <ref name="ref1"/>.. In conjunction with the c-Fos protein these two proteins bind to specific regions of DNA strands. Together these two proteins form the c-fos/c-jun complex which help regulate cell growth and differentiation <ref name="ref1"/>. Regulation of the complex iteslf is done by interactions between the protein and DNA in addition to the protein-protein interactions between each of the leucine zipper domains <ref name="ref1"/>. | ||
== Structure Overview == | |||
[[Image:1jun.png|thumb|Caption]] | |||
The structure of c-Jun is comprised of a leucine zipper as previously stated <ref name="ref2">.. this dimerization motif may be in one of two classes, both of which are required for DNA-binding transcription factors; the basic-domain leucine zipper proteins (bZIP) and the basic helix loop-helix-leucine zipper proteins (bHLH-ZIP)<ref name="ref2">. | |||
As can be been in the figure XXXXX, the strand becomes an elongated coiled coil. this is formed by residues at the a and d positions in each of the two monomers, whereby they create hydrophobic centers which conform to the "knobs into holes" model by Crick. <ref name="ref2">. amino acids at these a and d positions are each surrounded by 4 additional residues from adjacent a-helix monomer <ref name="ref2">. | As can be been in the figure XXXXX, the strand becomes an elongated coiled coil. this is formed by residues at the a and d positions in each of the two monomers, whereby they create hydrophobic centers which conform to the "knobs into holes" model by Crick. <ref name="ref2">. amino acids at these a and d positions are each surrounded by 4 additional residues from adjacent a-helix monomer <ref name="ref2">. | ||
