C-JUN
From Proteopedia
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Revision as of 19:55, 30 March 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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The C-Jun protein belongs the member of the basic region leucine zippere (bZIP) family of transcription factors. All these factors bind to DNA as either homo or heterodimers [1]. This union of the two identical molecular units is mediated by each of their leucine zipper domains and subsequently a prerequisite to the binding of their related DNA enhancer elements [1]. This prerequisitie is needed as dimerization enables the alpha helical DNA binding domains to be inserted into adjacent grooves of the dyad symmetrical DNA recognition site. this therefore affects the activity of how these proteins are regulated by causing these protein to protein interactions between the leucine zipper domains in addition to the interactions between protein and DNA [1].
Introduction
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
