Sandbox Reserved 592: Difference between revisions

The catalytic domain is consisted of an alpha double helix. The double helix is located at the C-terminus end of the protein. The residue consisting the catalytic domain is about 82-100 amino acids long (Shown in Figure 2). The C-terminus is where the transfer of the methyl group to the lysine residue occurs. In addition to the two main domains to the enzyme, there is an essential hydrophobic core which is very similar to other chromodomain proteins. The hydrophobic core is made up several residues. These residues are V45, L48, Y60, V62, W64, L80, I85 and L86 (Shown in Figure 2).<scene name='Sandbox_Reserved_592/Essential_hydrophobic_core/1'>TextToBeDisplayed</scene> The groove formed by the beta sheets is also similar and conserved feature of the chromodomain family. The physical characteristics between the chromodomain of SUV39h1 and chromodomains of other enzymes are very similar. SUV39h1 has been shown to very similar to the chromodomain of MPP8 and HP1, showing a conservation in chromodomain structure (shown in Figure 3). Although the chromodomain structure is very similar, there is a slight difference with the catalytic domain being longer. In addition to the catalytic domain of SUV39H1 being longer, the enzyme contains a F34 aromatic cage, which was originally thought to be essential for recognizing exposed lysine or argon residue. However, crystallography of residues (44-106) has shown residues missing the F34 aromatic cage.