Sandbox Reserved 1717: Difference between revisions

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==Significant Cysteines==

A set of four cysteines is consistently conserved in all VKOR homologs. In the human homolog (HsVKOR) these cysteines are Cys43, Cys51, Cys132, and Cys 135. <scene name='90/~~904321~~/Cysteines/3'>Significant ~~Cysteines~~</scene> In the Pufferfish homolog (TrVKORL) these cysteines, due to Cryo-EM differences,are Cys52, Cys55, Cys141, and Cys144. These cysteines are the key factor that allow for Vitamin K Epoxide Reductase to perform its function, which is to open the epoxide ring on Vitamin K Epoxide in order to re-make Vitamin K Quinone. In the closed conformation, that is induced when Vitamin K binds in the hydrophobic pocket, Cys-132 binds to Cys-51 and Cys-135 will bind to the 3' hydroxyl group on Vitamin K Epoxide, which allows for the electron transfer to open up the epoxide ring. <scene name='90/904321/Cys52disulfidecys55/4'>TrVKORL Cysteine Bonded to Vitamin K Epoxide</scene>

A set of four cysteines is consistently conserved in all VKOR homologs. In the human homolog (HsVKOR) these cysteines are Cys43, Cys51, Cys132, and Cys 135. <scene name='90/904322/Cysteines/1'>Significant cysteines</scene> In the Pufferfish homolog (TrVKORL) these cysteines, due to Cryo-EM differences,are Cys52, Cys55, Cys141, and Cys144. These cysteines are the key factor that allow for Vitamin K Epoxide Reductase to perform its function, which is to open the epoxide ring on Vitamin K Epoxide in order to re-make Vitamin K Quinone. In the closed conformation, that is induced when Vitamin K binds in the hydrophobic pocket, Cys-132 binds to Cys-51 and Cys-135 will bind to the 3' hydroxyl group on Vitamin K Epoxide, which allows for the electron transfer to open up the epoxide ring. <scene name='90/904321/Cys52disulfidecys55/4'>TrVKORL Cysteine Bonded to Vitamin K Epoxide</scene>

Sandbox Reserved 1717: Difference between revisions

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Revision as of 18:42, 29 March 2022 view source Bianca Pontrelli (talk \| contribs) 89 edits No edit summary ← Older edit		Revision as of 18:50, 29 March 2022 view source Bianca Pontrelli (talk \| contribs) 89 edits No edit summary Newer edit →
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	==Significant Cysteines==		==Significant Cysteines==

	A set of four cysteines is consistently conserved in all VKOR homologs. In the human homolog (HsVKOR) these cysteines are Cys43, Cys51, Cys132, and Cys 135. <scene name='90/~~904321~~/Cysteines/3'>Significant ~~Cysteines~~</scene> In the Pufferfish homolog (TrVKORL) these cysteines, due to Cryo-EM differences,are Cys52, Cys55, Cys141, and Cys144. These cysteines are the key factor that allow for Vitamin K Epoxide Reductase to perform its function, which is to open the epoxide ring on Vitamin K Epoxide in order to re-make Vitamin K Quinone. In the closed conformation, that is induced when Vitamin K binds in the hydrophobic pocket, Cys-132 binds to Cys-51 and Cys-135 will bind to the 3' hydroxyl group on Vitamin K Epoxide, which allows for the electron transfer to open up the epoxide ring. <scene name='90/904321/Cys52disulfidecys55/4'>TrVKORL Cysteine Bonded to Vitamin K Epoxide</scene>		A set of four cysteines is consistently conserved in all VKOR homologs. In the human homolog (HsVKOR) these cysteines are Cys43, Cys51, Cys132, and Cys 135. <scene name='90/904322/Cysteines/1'>Significant cysteines</scene> In the Pufferfish homolog (TrVKORL) these cysteines, due to Cryo-EM differences,are Cys52, Cys55, Cys141, and Cys144. These cysteines are the key factor that allow for Vitamin K Epoxide Reductase to perform its function, which is to open the epoxide ring on Vitamin K Epoxide in order to re-make Vitamin K Quinone. In the closed conformation, that is induced when Vitamin K binds in the hydrophobic pocket, Cys-132 binds to Cys-51 and Cys-135 will bind to the 3' hydroxyl group on Vitamin K Epoxide, which allows for the electron transfer to open up the epoxide ring. <scene name='90/904321/Cys52disulfidecys55/4'>TrVKORL Cysteine Bonded to Vitamin K Epoxide</scene>