Kwon sandbox: Difference between revisions

==Research of Structure and Function==  

There are two main structures of the c-Myc proteins that are significant in its function.  These are the Thr58 sight and the helix-loop-helix (HLH) motif surrounded by a basic amino acid region and a leucine zipper motif.

Kandil and colleagues speculated that the carboxyl terminus of the c-Myc protein had a similar structure to that of the helix-loop-helix family of DNA-binding proteins.  Their research showed that the helix-loop-helix structure was in fact the DNA binding domain of c-Myc and were able to establish the corresponding binding sequence as GACCACGTGGTC.  This sequence was found to be present in regulatory regions of genes during replication.  They compared DNA binding of c-Myc to HLH protein TFEB.  They found that the two proteins had the same inner nucleotides, providing significant evidence of the homology.  Kandil and colleagues then placed spacing between half-sites of the DNA binding site.  The inability of c-Myc to bind to the altered site provided evidence that c-Myc dimerizes when bound to DNA.   

Bahram and colleagues found that the mutation of Thr58 in c-Myc was prevalent in many cancers.  They then researched the effect of Thr58 mutation and found that it was the ubiquitination site of the protein.  Their in vitro experiment showed that c-Myc with Thr58 mutation had a longer turnover rate than wild type c-Myc.  They also found that histadine-tagged ubiquitin octamers were unable to bind to Thr58 mutant c-Myc proteins but successfully did bind to wild type.  This provided strong evidence that the site is indeed the ubiquitination site.