Sandbox Reserved 488

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Revision as of 01:32, 1 May 2012 by Thien Tran (Talk | contribs)
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This Sandbox is Reserved from 13/03/2012, through 01/06/2012 for use in the course "Proteins and Molecular Mechanisms" taught by Robert B. Rose at the North Carolina State University, Raleigh, NC USA. This reservation includes Sandbox Reserved 451 through Sandbox Reserved 500.
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c-Myc Protein

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Background

c-Myc protein, also known as Transcription factor p64, is a product of the c-myc proto-oncogene that has the ability to bind to DNA and regulate gene transcription. More specifically, c-Myc recognizes the DNA's core sequence 5'-CAC[GA]TG-3' by forming a heterodimer with MAX, a bHLh protein. This structure then interact with TAF1C, SPAG9,PARP10, KDM5A, and KDM5B. This protein is found mainly in Human and it's known to express the MYC gene using an E.coli expression host.


Structure

The c-myc gene is consisted of three exons located on human chromosomes 8q24. The c-Myc sequence contains many Myc boxes, or conserved N-terminal domains, which are found in N-Myc and L-Myc. The C-terminal region of c-Myc contains the helix-loop-helix, leucine zipper, and a basic region. These three components dimerize to form a bHLH LZ motif. The binding of DNA is achieved by the combination of the bHLH LZ motif and another bHLH LZ protein, Max.

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