Sandbox Reserved 1709: Difference between revisions

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== Structural Highlights==

=== Active Site ===

Within the four transmembrane helices lies the active site. The active site is comprised of a hydrophobic pocket containing two hydrophilic residues, A80 and Y139, that interact with substrates and ligands alike. The hydrophobic pocket provides specificity to the region while the hydrophilic residues have potential to hydrogen bond, allowing recognition and increasing specificity as well. Slightly above the active site is a crucial disulfide bridge that provides stabilization when a substrate is bound. This bridge occurs between C132 and C135, recurrent residues that continually aid in VKOR function.

Within the four transmembrane helices lies the <scene name='90/906893/Active_site/4'>active site</scene>. The active site is comprised of a hydrophobic pocket containing two hydrophilic residues, A80 and Y139, that interact with substrates and ligands alike. The hydrophobic pocket provides specificity to the region while the hydrophilic residues have potential to hydrogen bond, allowing recognition and increasing specificity as well. Slightly above the active site is a crucial disulfide bridge that provides stabilization when a substrate is bound. This bridge occurs between C132 and C135, recurrent residues that continually aid in VKOR function.

The active site plays a vital role in binding of any substrate or ligand to the VKOR. Upon binding, the VKOR will transition into a <scene name='90/906893/Closed_conformation/4'>closed conformation</scene> that will allow its catalytic mechanism to commence.

The <scene name='90/906893/Active_site/2'>active site</scene> plays a vital role in binding of any substrate or ligand to the VKOR. Upon binding, the VKOR will transition into a <scene name='90/906893/Closed_conformation/4'>closed conformation</scene> that will allow its catalytic mechanism to commence.

=== Cap Domain ===

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=== Mutations ===

Some key <scene name='90/906893/Active_site_mutations/1'>mutations</scene> that can be detrimental to the VKOR structure are mutations of the <scene name='90/906893/Active_site/2'>active site</scene>. The two main residues, N80 and Y139, can be mutated to A80 and F139 creating a decrease in recognition and stabilization

Some key <scene name='90/906893/Active_site_mutations/2'>mutations</scene> that can be detrimental to the VKOR structure are mutations of the <scene name='90/906893/Active_site/4'>active site</scene>. The two main residues, N80 and Y139, can be mutated to A80 and F139 creating a decrease in recognition and stabilization.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>

Sandbox Reserved 1709: Difference between revisions

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@@ Line 11: / Line 11: @@
 == Structural Highlights==
 === Active Site ===
-Within the four transmembrane helices lies the active site. The active site is comprised of a hydrophobic pocket containing two hydrophilic residues, A80 and Y139, that interact with substrates and ligands alike. The hydrophobic pocket provides specificity to the region while the hydrophilic residues have potential to hydrogen bond, allowing recognition and increasing specificity as well. Slightly above the active site is a crucial disulfide bridge that provides stabilization when a substrate is bound. This bridge occurs between C132 and C135, recurrent residues that continually aid in VKOR function.
+Within the four transmembrane helices lies the <scene name='90/906893/Active_site/4'>active site</scene>. The active site is comprised of a hydrophobic pocket containing two hydrophilic residues, A80 and Y139, that interact with substrates and ligands alike. The hydrophobic pocket provides specificity to the region while the hydrophilic residues have potential to hydrogen bond, allowing recognition and increasing specificity as well. Slightly above the active site is a crucial disulfide bridge that provides stabilization when a substrate is bound. This bridge occurs between C132 and C135, recurrent residues that continually aid in VKOR function.
+The active site plays a vital role in binding of any substrate or ligand to the VKOR. Upon binding, the VKOR will transition into a <scene name='90/906893/Closed_conformation/4'>closed conformation</scene> that will allow its catalytic mechanism to commence.
-The <scene name='90/906893/Active_site/2'>active site</scene> plays a vital role in binding of any substrate or ligand to the VKOR. Upon binding, the VKOR will transition into a <scene name='90/906893/Closed_conformation/4'>closed conformation</scene> that will allow its catalytic mechanism to commence.
 === Cap Domain ===
@@ Line 38: / Line 39: @@
 === Mutations ===
-Some key <scene name='90/906893/Active_site_mutations/1'>mutations</scene> that can be detrimental to the VKOR structure are mutations of the <scene name='90/906893/Active_site/2'>active site</scene>. The two main residues, N80 and Y139, can be mutated to A80 and F139 creating a decrease in recognition and stabilization
+Some key <scene name='90/906893/Active_site_mutations/2'>mutations</scene> that can be detrimental to the VKOR structure are mutations of the <scene name='90/906893/Active_site/4'>active site</scene>. The two main residues, N80 and Y139, can be mutated to A80 and F139 creating a decrease in recognition and stabilization.
-This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
 </StructureSection>