C-JUN
From Proteopedia
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== Introduction == | == Introduction == | ||
| - | + | This protein is a dimer that is completely symmetrical (a). It is comprised of coiled coil of two alpha helices (a). | |
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== Structural Overview == | == Structural Overview == | ||
Revision as of 11:06, 26 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. |
Contents |
C-JUN
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. (c). 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 (c). 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 (c).
Introduction
This protein is a dimer that is completely symmetrical (a). It is comprised of coiled coil of two alpha helices (a).
Structural Overview
Protein Function
OTHER
References
| 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. |
Proteopedia Page Contributors and Editors (what is this?)
Andrew Rebeyka, Michal Harel, Alexander Berchansky, David Canner, Andrea Gorrell
