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Medicine Research ›› 2019, Vol. 3 ›› Issue (3): 190012-0.DOI: 10.21127/yaoyimr20190012

• • 上一篇    下一篇

Insights into the Structure of Human Blood Coagulation Factor Ⅹ

Quan Shen, Pengjie Tang, Ming Ma, and Bin Bao*   

  1. Department of Marine Bio-Pharmacology, College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China
  • 收稿日期:2019-11-29 修回日期:2019-12-17 出版日期:2019-12-20 发布日期:2020-02-01
  • 基金资助:
     

Insights into the Structure of Human Blood Coagulation Factor Ⅹ

Quan Shen, Pengjie Tang, Ming Ma, and Bin Bao*   

  1. Department of Marine Bio-Pharmacology, College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China
  • Received:2019-11-29 Revised:2019-12-17 Online:2019-12-20 Published:2020-02-01
  • Contact: bbao@shou.edu.cn (B. B.)
  • Supported by:
     

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摘要： The solution structure and function of human coagulation factor X (FX) were studied to understand the key structural elements of the enzyme form during activation. FX is a vitamin K-dependent plasma glycoprotein, composed of light and heavy chains, and plays a central role in the coagulation cascade. The calcium-rich γ-carboxyglutamic acid domain is responsible for binding to the membrane, an important step in the coagulation process. After activation, the serine protease domain undergoes a significant relocation, forming a compact multidomain. The S1-specific pocket largely determines the functional activities that activate FX. The enzyme-producing form of FX is more extensive than the active form. The enzyme-producing and activated forms of FX have different conformations in the serine protease domain.

 

关键词: factor Ⅹ, factor Xa, serine protease domain, γ-carboxyglutamic acid domain, differences

Abstract: The solution structure and function of human coagulation factor X (FX) were studied to understand the key structural elements of the enzyme form during activation. FX is a vitamin K-dependent plasma glycoprotein, composed of light and heavy chains, and plays a central role in the coagulation cascade. The calcium-rich γ-carboxyglutamic acid domain is responsible for binding to the membrane, an important step in the coagulation process. After activation, the serine protease domain undergoes a significant relocation, forming a compact multidomain. The S1-specific pocket largely determines the functional activities that activate FX. The enzyme-producing form of FX is more extensive than the active form. The enzyme-producing and activated forms of FX have different conformations in the serine protease domain.

Key words: factor Ⅹ, factor Xa, serine protease domain, γ-carboxyglutamic acid domain, differences

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