A paper shedding new light on the earliest molecular stages of mammals’ vision process has recently been published in the Nature journal. The authors include Dr Przemysław Nogły from the Dioscuri Centre for Structural Dynamics and Receptors at the Faculty of Biochemistry, Biophysics and Biotechnology of the Jagiellonian University.
The article 'Ultrafast structural changes direct the first molecular events of vision' is devoted to the structural changes that take place in a rhodopsin molecule as a result of the absorption of light by 11-cis-retinal - a ligand covalently bound with protein. The published results are the conclusion of long-time studies conducted by researchers from the Paula Scherrer Institute in Switzerland.
Thanks to the use of the time-resolved serial femtosecond crystallography using X-ray free-electron lasers, the scientists were able to obtain information about the room temperature structure of rhodopsin 1 picosecond and 100 picoseconds after light activation. It turned out that retinal isomerisation results in the weakening of numerous van der Waals interactions between ligands and amino acids from the binding pocket, and as a result of relaxation the receptor undergoes conformation change, which allows interactions with G proteins and further transmission of the signal at later stages.
According to the JU Faculty of Biochemistry, Biophysics and Biotechnology (FBBB), the results of the study lay an experimental basis for the research into early activation events in the large family of class A GPCR proteins.
It is worth noting that the authors of the article also include Filip Pamuła, a Biochemistry graduate who gained his first experiences with the GPCR receptors as an MSc student of the Department of Physical Biochemistry at the JU FBBB, under the supervision of Dr hab. Agnieszka Polit, Prof. UJ.
