C-JUN: Difference between revisions
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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">. 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">. | |||
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 03:50, 1 April 2010
Andrew Rebeyka
C-JUN
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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 Cite error: Closing </ref> missing for <ref> tag.
It is comprised of a coiled coil of two alpha helices <ref name="ref2">.
C-Jun binds to specific DNA sites either in the homodimer or deterodimer forms with the aid of C-Fos protein [1]. C-Jun is a transcriptional activator [1]. C-jun, with the aid of C-Fos represents a crucial union between normal and uncontrolled cell growth as their combined role in the transduction of afferent growth signals the response of specific genes [1].
Protein Function
OTHER
References
- ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 Junius FK, O'Donoghue SI, Nilges M, Weiss AS, King GF. High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer. J Biol Chem. 1996 Jun 7;271(23):13663-7. PMID:8662824
- ↑ Cite error: Invalid
<ref>tag; no text was provided for refs namedXXX
Proteopedia Page Contributors and Editors (what is this?)
Andrew Rebeyka, Andrea Gorrell, Michal Harel, Alexander Berchansky, David Canner
