Sandbox Reserved 592: Difference between revisions

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== Structure ==

=== SET Structure ===

There is a chromodomain and SET domain. The SET is known as the catalytic ~~domainThe~~ 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) <ref>PMID:23285239</ref>. <scene name='Sandbox_Reserved_592/Essential_hydrophobic_core/2'>Essential_hydrophobic_core</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 does not contain 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. Instead, it has W64 and Y67 which form a loop; this is also another conserved feature among chromodomain family <ref>PMID:19234526</ref>.

There is a chromodomain and SET domain. The SET is known as the catalytic domain. 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 (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) <ref>PMID:23285239</ref>. <scene name='Sandbox_Reserved_592/Essential_hydrophobic_core/2'>Essential_hydrophobic_core</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 does not contain 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. Instead, it has W64 and Y67 which form a loop <scene name='Sandbox_Reserved_592/W64_and_w67_loop/1'>W64_and_w67_loop</scene>; this is also another conserved feature among chromodomain family <ref>PMID:19234526</ref>.

[[Image:YFP.jpg| 400 px | thumb |left| Figure 3: For Figure a, b, and c, these represents SUV39H1, MPP8 and HP1 respectively.]]

=== Chromodomain Structure ===

Crystal structure shows two main parts to the protein, but as a whole three independent tertiary protein molecules. 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 44-50 amino acids ~~long~~, which forms three anti- parallel beta sheets. The residues 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.<scene name='Sandbox_Reserved_592/Beta_sheets_of_suv39h1/2'>Beta_sheets_of_suv39h1</scene>

Crystal structure shows two main parts to the protein, but as a whole three independent tertiary protein molecules. 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 44-50 amino acids, which forms three anti- parallel beta sheets. The residues for each of three beta sheets are 45-53, 58-64 and 73-76 amino acids for beta 1, beta 2 and beta 3, respectively ( shown in figure 2). These three beta sheets form the chromodomain.<scene name='Sandbox_Reserved_592/Beta_sheets_of_suv39h1/2'>Beta_sheets_of_suv39h1</scene>

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 == Structure ==
 === SET Structure ===
-There is a chromodomain and SET domain. The SET is known as the catalytic domainThe 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) <ref>PMID:23285239</ref>. <scene name='Sandbox_Reserved_592/Essential_hydrophobic_core/2'>Essential_hydrophobic_core</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 does not contain 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. Instead, it has W64 and Y67 which form a loop; this is also another conserved feature among chromodomain family <ref>PMID:19234526</ref>.
+There is a chromodomain and SET domain. The SET is known as the catalytic domain. 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 (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) <ref>PMID:23285239</ref>. <scene name='Sandbox_Reserved_592/Essential_hydrophobic_core/2'>Essential_hydrophobic_core</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 does not contain 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. Instead, it has W64 and Y67 which form a loop <scene name='Sandbox_Reserved_592/W64_and_w67_loop/1'>W64_and_w67_loop</scene>; this is also another conserved feature among chromodomain family <ref>PMID:19234526</ref>.
 [[Image:YFP.jpg| 400 px | thumb |left| Figure 3: For Figure a, b, and c, these represents SUV39H1, MPP8 and HP1 respectively.]]
 <Structure load='3mts' size='400' frame='true' align='middle' caption='3-D structure of SUV39H1' scene='Insert optional scene name here' />
 === Chromodomain Structure ===
-Crystal structure shows two main parts to the protein, but as a whole three independent tertiary protein molecules.  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 44-50 amino acids long, which forms three anti- parallel beta sheets. The residues 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.<scene name='Sandbox_Reserved_592/Beta_sheets_of_suv39h1/2'>Beta_sheets_of_suv39h1</scene>
+Crystal structure shows two main parts to the protein, but as a whole three independent tertiary protein molecules.  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 44-50 amino acids, which forms three anti- parallel beta sheets. The residues for each of three beta sheets are 45-53, 58-64 and 73-76 amino acids for beta 1, beta 2 and beta 3, respectively ( shown in figure 2). These three beta sheets form the chromodomain.<scene name='Sandbox_Reserved_592/Beta_sheets_of_suv39h1/2'>Beta_sheets_of_suv39h1</scene>
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