Citation: CHEN Song, WANG Yu, ZHAO Bao-Yu, CHEN Zhuo, HUANG Ming-Dong. Maltose-binding Protein Improving the Crystallizability of C2 Domain of Human Coagulation Factor V[J]. Chinese Journal of Structural Chemistry, ;2014, 33(2): 216-222. shu

Maltose-binding Protein Improving the Crystallizability of C2 Domain of Human Coagulation Factor V

CHEN Song ^a,b ,
WANG Yu ^a,b ,
ZHAO Bao-Yu ^a,b ,
CHEN Zhuo ^a ,
HUANG Ming-Dong ^a,,

1.
a State Key Laboratory of Structural Chemistry, Fujian Institute of Research on the Structure of Matter, Chinese Academy of Sciences, Fuzhou 350002, China;
2.
b Graduate School of Chinese Academy of Sciences, Beijing 100039, China

Corresponding author: HUANG Ming-Dong,
Received Date: 4 June 2013
Available Online: 27 November 2013
Fund Project: Supported by the National Natural Science Foundation of China (31161130356) (31161130356)

Human coagulation Factor V (FV), together with Factor Xa, assembles to prothrombi-nase complex on activated cell surface, which converts prothrombin into thrombin, leading to fibrin deposition. The C2 domain of FV is believed to be a primary anchor for the assembly of prothrombinase on the cell surface, and was proposed as a target to intervene with pathological thrombotic events. We report here the crystal structure of the C2 domain of FV fused to maltose-binding protein (MBP). The fusion tag of MBP is critical to generate the crystal for this study. There is no strong interaction between MBP and FVC2. The overall structure of FVC2 is similar to the previous FVC2 structures, suggesting the MBP fusion does not perturb the molecular structure of FVC2. This crystal form of FVC2 can be used for future study of molecular interaction between FVC2 and its inhibitors.
- maltose-binding protein,
- coagulation factor V,
- protein crystallizability
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