Sandbox Reserved 1709: Difference between revisions

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<scene name='90/906893/Vkor_structure/1'>Vitamin K epoxide reductase</scene> (VKOR) is an enzyme that, as its name implies, promotes the reduction of <scene name='90/906893/Vkor_with_ko/1'>vitamin K epoxide</scene> (KO). VKOR is a transmembrane protein spanning the endoplasmic reticulum and composed of  [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2919313/ 4 transmembrane helical proteins]. One of its primary roles is to assist in blood coagulation by regenerating hydroquinone (KH2). KH2 acts as a γ-carboxylase cofactor that drives the γ-carboxylation of several coagulation factors. Structural characterization of VKOR has been difficult, though, due to its in vitro instability. Nonetheless, a near perfect atomic structure has been determined utilization anticoagulant stabilization and VKOR-like [https://pubmed.ncbi.nlm.nih.gov/33154105/ homologs].
<scene name='90/906893/Vkor_structure/1'>Vitamin K epoxide reductase</scene> (VKOR) is an enzyme that, as its name implies, promotes the reduction of <scene name='90/906893/Vkor_with_ko/1'>vitamin K epoxide</scene> (KO). VKOR is a transmembrane protein spanning the endoplasmic reticulum and composed of  [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2919313/ 4 transmembrane helical proteins]. One of its primary roles is to assist in blood coagulation by regenerating hydroquinone (KH2). KH2 acts as a γ-carboxylase cofactor that drives the γ-carboxylation of several coagulation factors. Structural characterization of VKOR has been difficult, though, due to its in vitro instability. Nonetheless, a near perfect atomic structure has been determined utilization anticoagulant stabilization and VKOR-like [https://pubmed.ncbi.nlm.nih.gov/33154105/ homologs].
   
   
[[Image:VKOR_mechanism_2D.png |500 px|right| thumb]]
[[Image:VKOR_mechanism_2D.png |500 px|right|thumb|Figure 1. Structures of VKOR 2D manipulation for Vitamin K activation]]
=== Author's Notes ===  
=== Author's Notes ===  
As previously mentioned, the VKOR structure has been challenging to qualify. Thus it is important to note that to date all VKOR structures discovered were done so from 2 methods. First, crystal structures of Human VKOR were captured with a bound substrate (KO) or vitamin K antagonist (VKA). VKA substrates utilized were anticoagulants, namely Warfarin, brodifacoum, phenindione, and chlorophacinone. Second, VKOR-like homologs, specifically isolated from the pufferfish ''Takifugu rubripes'', aided in structure classification as well.  
As previously mentioned, the VKOR structure has been challenging to qualify. Thus it is important to note that to date all VKOR structures discovered were done so from 2 methods. First, crystal structures of Human VKOR were captured with a bound substrate (KO) or vitamin K antagonist (VKA). VKA substrates utilized were anticoagulants, namely Warfarin, brodifacoum, phenindione, and chlorophacinone. Second, VKOR-like homologs, specifically isolated from the pufferfish ''Takifugu rubripes'', aided in structure classification as well.  
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