Sandbox Reserved 592: Difference between revisions
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=== Chromodomain Structure === | === Chromodomain Structure === | ||
Crystal structure shows two main parts to the protein, but as a whole three independent molecules. There is a chromodomain and SET domain. The chromodomain starts at the N-terminus of the enzyme and continues toward the C-terminus, where the SET catalytic domain is located. The chromodomain length is around 44-106 amino acids long, which forms three | Crystal structure shows two main parts to the protein, but as a whole three independent molecules. There is a chromodomain and SET domain. The chromodomain starts at the N-terminus of the enzyme and continues toward the C-terminus, where the SET catalytic domain is located. The chromodomain length is around 44-106 amino acids long, which forms three anti- parallel beta sheets. The lengths for each of three beta sheets are 45-53, 58-64 and 73-76 amino acids long for beta 1, beta 2 and beta 3, respectively ( shown in figure 2). These three beta sheets form the chromodomain. | ||
=== SET Structure === | === SET Structure === | ||
The catylatic domain is consisted of a alpha doible helix. The double helix is located on the C-terminus end of the portein. The residue consisting the catylatic domain is about 82-100 amino acids long. 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 reisdues are V45, L48, Y60, V62, W64, L80, I85 and L86 (each letter represents an amino acids). The similarity between the chromodomain of SUV39h1 and chromodomains of other enzymes is very similar. SUV39h1 has been shown to very similar to the chromoddomain of MPP8 and HP1, showing a conservation in chromodomain structure. although the chromodomain structure is very similar, there is a slight difference with the catylitic domain being longer. In addition to the catyltic domain of SUV39H1 being longer, The enzyme lacks a F34 aromatic cage, which was originally thought to be essential for recognizing exposed lysine or argon residue. However, residues of form a loop which binds to the exposed rsidues of the substrate, showing that it is not a conserved feature in the chromodomain family of enzymes. | The catylatic domain is consisted of a alpha doible helix. The double helix is located on the C-terminus end of the portein. The residue consisting the catylatic domain is about 82-100 amino acids long. 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 reisdues are V45, L48, Y60, V62, W64, L80, I85 and L86 (each letter represents an amino acids). The similarity between the chromodomain of SUV39h1 and chromodomains of other enzymes is very similar. SUV39h1 has been shown to very similar to the chromoddomain of MPP8 and HP1, showing a conservation in chromodomain structure. although the chromodomain structure is very similar, there is a slight difference with the catylitic domain being longer. In addition to the catyltic domain of SUV39H1 being longer, The enzyme lacks a F34 aromatic cage, which was originally thought to be essential for recognizing exposed lysine or argon residue. However, residues of form a loop which binds to the exposed rsidues of the substrate, showing that it is not a conserved feature in the chromodomain family of enzymes. | ||
