The world's strongest X-ray laser crack cell signaling password
July 28, 2017 Source: Web of Science Author: Zhu Tailai
Window._bd_share_config={ "common":{ "bdSnsKey":{ },"bdText":"","bdMini":"2","bdMiniList":false,"bdPic":"","bdStyle":" 0","bdSize":"16"},"share":{ }};with(document)0[(getElementsByTagName('head')[0]||body).appendChild(createElement('script')) .src='http://bdimg.share.baidu.com/static/api/js/share.js?v=89860593.js?cdnversion='+~(-new Date()/36e5)];The international cross-team led by researcher Xu Huaqiang of the Shanghai Institute of Materia Medica of the Chinese Academy of Sciences has successfully solved the crystal structure of the phosphorylated rhodopsin and Arrestin complexes and solved the phosphoric acid responsible for shutting down the GPCR signal. Password. On July 27th, relevant research results were published in the journal Cell in the cover article.
The function of life is embodied or executed by means of a signalling code. G protein-coupled receptors (GPCRs) are the largest family of cell membrane surface receptors in the human body. They are responsible for the "signal soldiers" of cell signal transduction through the two major signaling pathways of G protein and repressor. When stimulated by external signals, the GPCR activates the G protein to emit an "open" signal. The "off" signal is derived from the phosphorylation code - once the GPCR tail is phosphorylated, the repressor is activated and tightly bound to form a complex, thereby turning off the conduction signal. Therefore, the identification and interpretation of GPCR phosphorylation codes is an important scientific issue in the field of cell signaling today.
It is reported that the cross-team led by Xu Huaqiang successfully analyzed the complete complex structure of GPCR and repressor protein complex in 2015, and developed a solution to the high-resolution structure and phosphorylation mechanism of the tail of the structure.
“We used the world's strongest X-ray laser to see the tail structure information of the composite crystal, and analyzed the process of tail phosphorylation recruitment and binding to the repressor protein.†Xu Huaqiang likened the research process to the layer of life code. Layer decryption, "In order to verify the universality of the phosphorylation code, we tested 96% of the GPCR proteins and found that the "off" signals of 70%-80% of GPCRs were controlled by phosphorylation codes." Finally, through a series of validation biology Functional verification, the GPCR recruits the phosphorylation codon of the repressor protein to this effect - GPCR recruits through the phosphorylation of its tail amino acid and binds to the repressor protein, and found that the code is universal for the entire GPCR proteome.
It is understood that major breakthroughs in structural biology are often closely related to the combination of synchrotron radiation sources and X-ray free electron lasers. There are currently six such combinations in the world, located in Germany, the United States, Japan, South Korea, Switzerland and Italy. "We are very much looking forward to China's own major technological infrastructure, such as soft X-ray and hard X-ray free electron laser devices under construction and promotion." Xu Huaqiang said, "These large scientific platforms can provide scientists with more advanced and richer Comprehensive experimental means."
According to reports, this research has been funded by the National Fund for Major Major Drug Creation, 973, Pilot Project and International Projects. Cooperative research institutions include the University of Toronto, the Scripps Research Institute, the Desy Free Electron Laser Science Center in Germany, the Ultrafast Imaging Center in Hamburg, the University of California, Los Angeles, the University of Southern California, the University of Shanghai, and the University of Vanderbilt.
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