The Nobel Prize in Chemistry in 2012 was won by two American scientists: Robert J. Lefkowitz and Brian K. Kobilka. Awarded for outstanding contributions in the field of research.
Among them, Brian K. Kobilka is currently a professor at the Stanford University School of Medicine and an academician of the American Academy of Sciences. He was hired as a "guest professor" at Tsinghua University in 2012. At present, he has completed the establishment of the laboratory of Tsinghua University School of Medicine and has begun to guide doctoral students and postdoctoral fellows. This scholar recently collaborated with Swiss scientists and published an article entitled “Cholesterol increases kinetic, energetic, and mechanical stability of the human β2-adrenergic receptor†in the American Proceedings of the National Academy of Sciences (PNAS) in November. For G protein-coupled receptors, what is the effect of cholesterol?
Cholesterol is an essential component of eukaryotic cell membranes and can functionally regulate membrane proteins, such as G protein-coupled receptors. However, scientists currently do not understand this specific regulatory process very well.
In order to analyze how cholesterol regulates the process of G protein-coupled receptors, in this article, the researchers used dynamic single-molecule force spectroscopy to quantitatively analyze the presence or absence of cholesterol analogs : Under the premise of cholesteryl hemisuccinate (CHS), the mechanical strength and flexibility of the human β2 adrenergic receptor (β2AR), conformational changes, and stable maintenance of the dynamic activity of the structural fragments of the receptor.
The study found that CHS can greatly enhance the kinetic energy and mechanical stability of almost every structural part. This enhancement is enough to change the structure and function of β2AR, but there is one exception, that is, the core part of the structure of β2AR. The body binding site, its characteristics have not been significantly affected by CHS.
Professor Kobilka has published many research results on G protein-coupled receptors. For example, this year his research group published three papers in a row, reporting the detailed crystal structure of the G protein-coupled receptor (GPCR) action complex, known as Wei is a truly breakthrough achievement.
The researchers used X-ray crystallographic technology to study the β2 adrenergic receptor complex coupled with G protein. According to reports, G protein is a protein composed of three different subunits It is easily separated from the GPCR protein and dissociated into three independent subunits, and the size of this complex is approximately twice that of the β2 adrenergic receptor protein. If you want to get the crystal structure of the β2 adrenergic receptor protein-G protein complex, you must first develop a new technology to purify the complex and make it stable, such as binding the complex to an antibody, or A series of experiments with different crystallization conditions and so on.
Because GPCR is a membrane protein—it penetrates the cell membrane up to 7 times and has many conformational morphologies, its structural biological analysis is not easy to carry out, and this article completed the X-ray crystal structure of the GPCR transmembrane signal action complex Many people have failed to complete the task, as Stephen Sprang of the University of Missouri said: This is a truly breakthrough article. For many years, people in our industry have dreamed of getting this structure chart, because It will eventually tell us how the GPCR receptor works.
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