New insight into receptor signalling
A team of 72 investigators across 25 institutions including researchers from the Paul Scherrer Institut obtained the X-ray structure of a rhodopsin–arrestin complex, which represents a major milestone in the area of G-protein-coupled-receptor (GPCR), a protein family recognized in the award of the 2012 Nobel Prize in Chemistry.
The study, “Crystal Structure of Rhodopsin Bound to Arrestin Determined by Femtosecond X-ray Laser”, which was published in the journal Nature, provides insight into the interactions between G-protein-coupled-receptors (GPCRs) and arrestins, proteins that regulate vital physiological functions such as sensory and hormonal responses. The GPCR rhodopsin is involved in one of the best-characterized GPCR signalling pathway that controls the process of visual phototransduction in the retina of the eye.
Many challenges were faced in the process of solving the X-ray structure of the rhodopsin–arrestin complex, in particular the very small and weakly diffracting crystals proved unsuitable for conventional synchrotron experiments. Only the ultrabright X-rays from the free-electron laser (FEL) at the SLAC National Accelerator Laboratory (Menlo Park, California) enabled the research team to obtain the structure at the atomic scale.
This finding represents an important step in designing new treatment against the many diseases that are mediated by GPCR signalling pathways, which are the target for almost half of the drugs currently on the market.
Such high-impact scientific discoveries will soon be possible at the new large-scale facility, SwissFEL, currently being built at the Paul Scherrer Institut.
Many challenges were faced in the process of solving the X-ray structure of the rhodopsin–arrestin complex, in particular the very small and weakly diffracting crystals proved unsuitable for conventional synchrotron experiments. Only the ultrabright X-rays from the free-electron laser (FEL) at the SLAC National Accelerator Laboratory (Menlo Park, California) enabled the research team to obtain the structure at the atomic scale.
This finding represents an important step in designing new treatment against the many diseases that are mediated by GPCR signalling pathways, which are the target for almost half of the drugs currently on the market.
Such high-impact scientific discoveries will soon be possible at the new large-scale facility, SwissFEL, currently being built at the Paul Scherrer Institut.