The article discusses the role of vitamin K-dependent -carboxylation of glutamate residues in various physiological functions, including hemostasis and immune response. The researchers used cryo-electron microscopy to reveal the structures of human VKGC, a key catalyst in this posttranslational modification. The study highlights how VKGC recognizes substrate proteins through specific interactions that trigger its activation, enabling the efficient carboxylation of proteins essential for health. Understanding this mechanism offers therapeutic insights into treating thromboembolic and hemorrhagic diseases.
The -carboxylation of glutamate residues by VKGC is crucial for various physiological functions, affecting hemostasis and calcium homeostasis among others.
Cryo-electron microscopy reveals that VKGC processes substrate proteins through knob-and-hole interactions, essential for its activation and carboxylation function.
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