Sandbox Reserved 1725: Difference between revisions

VKOR consists of four <scene name='90/904330/Transmembranehelices1/5'>transmembrane helices</scene> embedded in the endoplasmic reticulum membrane. The barrel domain was used experimentally to stabilize VKOR for structure determination (Figure 2)<ref name="Liu">PMID:33154105</ref>. For this page, the barrel domain has been removed and structures renumbered to correspond with the article by Liu. <ref name="Liu">PMID:33154105</ref>. Helices one and two are connected by the <scene name='90/904330/Betahairpin2/1'>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 <scene name='90/904330/Capdomain/1'>cap domain</scene> covering the active site, made up of an <scene name='90/904330/Capanchor/1'>anchor</scene>, <scene name='90/904330/Caploop/1'>loop</scene>, and <scene name='90/904330/Caphelix/1'>helix</scene>. 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>.