Sandbox Reserved 1725: Difference between revisions

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=== Structural Overview ===

VKOR consists of four <scene name='90/904330/Transmembranehelices1/5'>transmembrane helices</scene> embedded in the endoplasmic reticulum membrane. Helices one and two are ~~connected by~~ <scene name='90/904330/Betahairpin2/2'>Loop 1 and the beta hairpin</~~scene~~> region which contains two of the active cysteines, C43 and C51; these cysteines, along with C132 and C135, are essential for reduction and structural changes discussed in the next section<ref name="Liu">PMID:33154105</ref>. VKOR also has a cap domain consisting of a helix, loop, and anchor. The anchor serves to attach the cap domain to the ER membrane for stabilization<ref name="Liu">PMID:33154105</ref>. The loop helps stabilize one of the catalytic amino acids, Asn80<ref name="Liu">PMID:33154105</ref>. The helix is involved in stabilization of certain disulfide bonds and structural changes as part of the catalytic cycle discussed below<ref name="Liu">PMID:33154105</ref>.

VKOR consists of four <scene name='90/904330/Transmembranehelices1/5'>transmembrane helices</scene> embedded in the endoplasmic reticulum membrane. Helices one and two are <scene name='90/904330/Betahairpin2/2'>connected</scene> by Loop 1 and the beta hairpin region which contains two of the active cysteines, C43 and C51; these cysteines, along with C132 and C135, are essential for reduction and structural changes discussed in the next section<ref name="Liu">PMID:33154105</ref>. VKOR also has a cap domain consisting of a helix, loop, and anchor. The anchor serves to attach the cap domain to the ER membrane for stabilization<ref name="Liu">PMID:33154105</ref>. The loop helps stabilize one of the catalytic amino acids, Asn80<ref name="Liu">PMID:33154105</ref>. The helix is involved in stabilization of certain disulfide bonds and structural changes as part of the catalytic cycle discussed below<ref name="Liu">PMID:33154105</ref>.

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Sandbox Reserved 1725: Difference between revisions

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@@ Line 13: / Line 13: @@
 === Structural Overview ===
-VKOR consists of four <scene name='90/904330/Transmembranehelices1/5'>transmembrane helices</scene> embedded in the endoplasmic reticulum membrane. Helices one and two are connected by <scene name='90/904330/Betahairpin2/2'>Loop 1 and the beta hairpin</scene> region which contains two of the active cysteines, C43 and C51; these cysteines, along with C132 and C135, are essential for reduction and structural changes discussed in the next section<ref name="Liu">PMID:33154105</ref>. VKOR also has a cap domain consisting of a <b><span class="text-blue">helix</span></b>, <b><span class="text-green">loop</span></b>, and <b><span class="text-lightgreen">anchor</span></b>. The anchor serves to attach the cap domain to the ER membrane for stabilization<ref name="Liu">PMID:33154105</ref>. The loop helps stabilize one of the catalytic amino acids, Asn80<ref name="Liu">PMID:33154105</ref>. The helix is involved in stabilization of certain disulfide bonds and structural changes as part of the catalytic cycle discussed below<ref name="Liu">PMID:33154105</ref>.
+VKOR consists of four <scene name='90/904330/Transmembranehelices1/5'>transmembrane helices</scene> embedded in the endoplasmic reticulum membrane. Helices one and two are <scene name='90/904330/Betahairpin2/2'>connected</scene> by <b><span class="text-brown">Loop 1</span></b> and the <b><span class="text-orange">beta hairpin</span></b> region which contains two of the active cysteines, C43 and C51; these cysteines, along with C132 and C135, are essential for reduction and structural changes discussed in the next section<ref name="Liu">PMID:33154105</ref>. VKOR also has a cap domain consisting of a <b><span class="text-blue">helix</span></b>, <b><span class="text-lightmagenta">loop</span></b>, and <b><span class="text-olive">anchor</span></b>. The anchor serves to attach the cap domain to the ER membrane for stabilization<ref name="Liu">PMID:33154105</ref>. The loop helps stabilize one of the catalytic amino acids, Asn80<ref name="Liu">PMID:33154105</ref>. The helix is involved in stabilization of certain disulfide bonds and structural changes as part of the catalytic cycle discussed below<ref name="Liu">PMID:33154105</ref>.
 === Active Site ===