Your demand is our motivation !
Posted on 25th Mar 2015 @ 8:10 AM
Researchers from China Agricultural University, Chinese Academy of Medical Sciences of Beijing Union Medical College Hospital reported that they have developed a novel method , by using the fixed precipitating agent molecularly imprinted polymers (MIPs) to obtain the amino-terminal structure of human fragile X mental retardation protein (FMRP) . This important research result was published in the journal of "natural communication" (Nature Communications) on March 23 . Fragile X syndrome (fragile X syndrome, FXS) is hereditary mental retardation disease , whose incidence rate is second only to Down syndrome ,its incidence in men is 1/4 000 and 1/8 000 in females .The main clinical manifestations are : varying degrees of mental retardation, giant testicles, a special face, language development disorders and behavioral abnormalities (such as short attention span, clapping, avoiding eye contact) and so on.
FMRP is a multi-functional mRNA-binding protein encoded by X chromosome Fragile X mental retardation 1 (fmr1) gene , which could bind and regulate a variety of mRNA targeted transport and translation process in neuronal cytoplasm , and regulated expression of multiple functional protein in synapses . It is believed that fmr1 gene dynamic mutation triggered low FMRP protein may affect neuronal maturation and synaptic plasticity, ultimately resulted in FXS , seizures, cognitive dysfunction , mental disorders and other typical clinical symptoms Flexibility (Flexibility) is an inherent characteristic of the protein, it is essential for their biological functions. It is generally accepted that the area with larger flexibility is prone to occur conformational change, making protein molecules conformation unstable.
At present, it remains a challenge to obtain a high quality protein crystalline with different conformations The researchers developed a new method fixing the traditional precipitating agent on molecularly imprinted polymer can promote protein crystallization . This technique is particularly suitable for variable proteins. By using this method, they get a high-quality crystals of human FMRP protein flexible N- terminal. The researchers revealed a new KH domain and intramolecular disulfide bonds, and found several types of dimer in solution, thereby obtaining some new knowledge about the function of this protein. In addition, they also used this fixed precipitant MIPs (piMIPs) to successfully promote crystal formation of the variable protein, obtain five kinds of model proteins in a greater diffraction resolution .This highlights the enormous potential of piMIPs in variable protein crystallization.