Sandbox Reserved 1725: Difference between revisions
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==Protein Structure== | ==Protein Structure== | ||
=== Structural Overview === | === Structural Overview === | ||
VKOR consists of four <scene name='90/904330/Transmembranehelices1/5'>transmembrane helices</scene> embedded in the endoplasmic reticulum membrane (Figure 2). Helices one and two are <scene name='90/904330/Betahairpin2/ | VKOR consists of four <scene name='90/904330/Transmembranehelices1/5'>transmembrane helices</scene> embedded in the endoplasmic reticulum membrane (Figure 2). Helices one and two are <scene name='90/904330/Betahairpin2/5'>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, Cys43 and Cys51; these cysteines, along with Cys132 and Cys135, are essential for reduction and structural changes discussed in the next section<ref name="Liu">PMID:33154105</ref>. VKOR also has a <scene name='90/904330/Capdomain/3'>cap domain</scene> 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 <b><span class="text-olive">anchor</span></b> stabilizes the cap domain by attaching it to the surface of the ER membrane<ref name="Liu">PMID:33154105</ref>. The <b><span class="text-lightmagenta">loop</span></b> helps stabilize one of the substrate-binding amino acids, Asn80<ref name="Liu">PMID:33154105</ref>. The <b><span class="text-blue">helix</span></b> 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>. | ||
=== Author's Note === | === Author's Note === | ||