Sandbox Reserved 1709: Difference between revisions
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=Vitamin K Epoxide Reductase= | |||
<StructureSection load='VKORKO.pdb' size='340' side='right' caption='VKOR with KO bound.' scene='90/904314/Vkor_with_ko/2'> | <StructureSection load='VKORKO.pdb' size='340' side='right' caption='VKOR with KO bound.' scene='90/904314/Vkor_with_ko/2'> | ||
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=== Mutations === | === Mutations === | ||
Mutations of the <scene name='90/906893/Vkor_with_warfarin_bound/4'>active site residues</scene> can occur within the binding pocket of VKOR. These mutations can be detrimental to the VKOR structure and function<ref>DOI 10.1126/science.abc5667</ref>. Two of the most common mutations occur to residues N80 and Y139 mutating them to <scene name='90/906893/Active_site_mutations/3'>A80 and F139</scene>. The change in polarity of these mutations from polar to nonpolar will cause a decrease in recognition and stabilization due to the inability to provide hydrogen bonds. | Mutations of the <scene name='90/906893/Vkor_with_warfarin_bound/4'>active site residues</scene> can occur within the binding pocket of VKOR. These mutations can be detrimental to the VKOR structure and function<ref>DOI 10.1126/science.abc5667</ref>. Two of the most common mutations occur to residues N80 and Y139 mutating them to <scene name='90/906893/Active_site_mutations/3'>A80 and F139</scene>. The change in polarity of these mutations from polar to nonpolar will cause a decrease in recognition and stabilization due to the inability to provide hydrogen bonds to the substrate. | ||