C-JUN
From Proteopedia
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<applet load='1Z82' size='200' frame='true' align='right' caption='1JUN' /> | <applet load='1Z82' size='200' frame='true' align='right' caption='1JUN' /> | ||
Revision as of 03:12, 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. |
Contents |
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].
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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].
Structural Overview
This protein is a dimer that is completely symmetrical [2](a). It is comprised of coiled coil of two alpha helices [2]Proteopedia Page Contributors and Editors (what is this?)
Andrew Rebeyka, Michal Harel, Alexander Berchansky, David Canner, Andrea Gorrell
