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maltose-binding protein Improving the Crystallizability of C2 Domain of Human Coagulation Factor V

Chinese Journal of Structural Chemistry 2014年第2期33卷 216-222页

作者：陈松王宇赵宝玉陈卓黄明东 State Key Laboratory of Structural Chemistry Fujian Institute of Research on the Structure of Matter Chinese Academy of Sciences Graduate School of Chinese Academy of Sciences

Human coagulation Factor V（FV）, together with Factor Xa, assembles to prothrombinase 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 pro- thrombinase 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.

关键词： maltose-binding protein coagulation factor V protein crystallizability

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Purification of the Drosophila melanogaster proteins Inscuteable and Staufen Expressed in Escherichia coli

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Advances in Bioscience and Biotechnology 2015年第7期6卷 485-493页

作者： Xristo Zárate Megan M.McEvoy Teresa Vargas-Cortez Jéssica J.Gómez-Lugo Claudia J.Barahona Elena Cantú-Cárdenas Alberto Gómez-Trevino Universidad Autónoma de Nuevo León Facultad de Ciencias QuímicasCd.UniversitariaSan Nicolás de los GarzaMéxico Department of Chemistry and Biochemistry University of ArizonaTucsonUSA

The proteins Inscuteable and Staufen are key components during asymmetric cell division of neuroblasts for the development of Drosophila melanogaster. Expression and purification of both proteins has been a difficult task for structure-function studies. Based on codon optimization for protein expression in Escherichia coli, we have been able to produce, in soluble form, the C-terminal domains of Inscuteable and Staufen as chimeras with N-terminal maltose binding protein tag that contains a rigid linker between them for feasible crystallization. In addition, using an optimized synthetic gene, corresponding to the amino acid region 250 - 623 of Inscuteable fused to glutathione-S-transferase, low-scale expression experiments showed production of soluble protein. Finally, eukaryotic expression of Inscuteable in the methylothropic yeast Pichia pastoris failed to produce the Drosophila protein at detectable amounts, reinforcing the fact that E. coli still was the microorganism of choice for high-yield protein expression.

关键词： Inscuteable Staufen protein Expression and Purification maltose-binding protein Escherichia coli

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