C-JUN
From Proteopedia
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[[Image:1jun.png|left|thumb|'''Figure 1.''' A 3-D representation of the two alpha helices which form a coiled coil.<ref name="XXX"/>.]] | [[Image:1jun.png|left|thumb|'''Figure 1.''' A 3-D representation of the two alpha helices which form a coiled coil.<ref name="XXX"/>.]] | ||
| - | The structure of c-Jun is comprised of a leucine zipper as previously stated <ref name="ref2">. | + | 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">. | ||
Revision as of 03:49, 1 April 2010
Andrew Rebeyka
| Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. Andrea Gorrell. |
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Introduction
The c-Jun protein is a member of transcription factors which consist of a basic region leucine zipper region [1]. All these leucine zipper factors bind to DNA in one of two states: homo or heterodimers [1].. 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 [1]. 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 [1].
Structure Overview
The structure of c-Jun is comprised of a leucine zipper as previously stated [3].
It is comprised of a coiled coil of two alpha helices [3]Proteopedia Page Contributors and Editors (what is this?)
Andrew Rebeyka, Michal Harel, Alexander Berchansky, David Canner, Andrea Gorrell
