The course aims to provide the student with the key to understanding (tools, techniques, methods) the functioning of the main classes of cellular receptors, studying the structure and mechanisms of activation of the main classes of receptors at the molecular level. The course will held in hybrid session, with Aurora students allowed to follow on-line. The student will learn the molecular basis of the intrinsic activity of drugs, with particular reference to biotechnological drugs through a challenge-based approach, which, through the active involvement of the student in the analysis of the 3D structures of receptors, will stimulate critical learning in which the student will be confronted independently with the analysis of structures of drug-receptor complexes as well as the effects of changes in the structure of a drug on the biological activity of a receptor.
The course takes a challenge-based approach, based on the analysis of 3D receptors and ligand/receptors complexes. The students, in working groups using MS Teams, will have to tackle the analysis following the guidelines of the challenge. Through the flipped classroom approach, the working groups will have to present the results of the analyses to the class, effectively and using appropriate language.This approach will therefore not only provide an understanding of the structure-function relationships of receptors and the different approaches used to modulate their activity, but will also provide the student with tools and methods for analyzing protein structure. The student should be able to apply the methods of analysis to receptors not specifically addressed, and in general to the study of any protein structure.
For registration, please send an expression of interest to the professor.
Aurora is a partnership of like-minded and closely collaborating research‑intensive European universities, who use their academic excellence to drive societal change.
Co-funded by the Erasmus+ Programme of the European Union
This project has received funding from the European Union´s Horizon 2020 research and innovation programme under grant agreement No 101035804
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