The amino-terminal structure of human fragile X mental retardation protein obtained using precipitant-immobilized imprinted polymers

Yufeng Hu, Zhenhang Chen, Yanjun Fu, Qingzhong He, Lun Jiang, Jiangge Zheng, Yina Gao, Pinchao Mei, Zhongzhou Chen () and Xueqin Ren ()
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Yufeng Hu: College of Resources and Environmental Sciences, China Agricultural University
Zhenhang Chen: State Key Laboratory of Agrobiotechnology, China Agricultural University
Yanjun Fu: State Key Laboratory of Agrobiotechnology, China Agricultural University
Qingzhong He: National Key Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences and Peking Union Medical College
Lun Jiang: State Key Laboratory of Agrobiotechnology, China Agricultural University
Jiangge Zheng: State Key Laboratory of Agrobiotechnology, China Agricultural University
Yina Gao: State Key Laboratory of Agrobiotechnology, China Agricultural University
Pinchao Mei: National Key Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences and Peking Union Medical College
Zhongzhou Chen: State Key Laboratory of Agrobiotechnology, China Agricultural University
Xueqin Ren: College of Resources and Environmental Sciences, China Agricultural University

Nature Communications, 2015, vol. 6, issue 1, 1-11

Abstract: Abstract Flexibility is an intrinsic property of proteins and essential for their biological functions. However, because of structural flexibility, obtaining high-quality crystals of proteins with heterogeneous conformations remain challenging. Here, we show a novel approach to immobilize traditional precipitants onto molecularly imprinted polymers (MIPs) to facilitate protein crystallization, especially for flexible proteins. By applying this method, high-quality crystals of the flexible N-terminus of human fragile X mental retardation protein are obtained, whose absence causes the most common inherited mental retardation. A novel KH domain and an intermolecular disulfide bond are discovered, and several types of dimers are found in solution, thus providing insights into the function of this protein. Furthermore, the precipitant-immobilized MIPs (piMIPs) successfully facilitate flexible protein crystal formation for five model proteins with increased diffraction resolution. This highlights the potential of piMIPs for the crystallization of flexible proteins.

Date: 2015
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DOI: 10.1038/ncomms7634

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