Professional Education


  • Doctor of Philosophy, Universite De Paris Vii (2016)
  • Master of Science, Universita Degli Studi Di Milano (2013)
  • Laurea, Universita Degli Studi Di Milano (2010)
  • Master of Science, Academic Year Abroad (2013)

All Publications


  • Concerted conformational dynamics and water movements in the ghrelin G protein-coupled receptor ELIFE Louet, M., Casiraghi, M., Damian, M., Costa, M. S., Renault, P., Gomes, A. S., Batista, P. R., M'Kadmi, C., Mary, S., Cantel, S., Denoyelle, S., Salah, K., Perahia, D., Bisch, P. M., Fehrentz, J., Catoire, L. J., Floquet, N., Baneres, J. 2021; 10

    Abstract

    There is increasing support for water molecules playing a role in signal propagation through G protein-coupled receptors (GPCRs). However, exploration of the hydration features of GPCRs is still in its infancy. Here, we combined site-specific labeling with unnatural amino acids to molecular dynamics to delineate how local hydration of the ghrelin receptor growth hormone secretagogue receptor (GHSR) is rearranged upon activation. We found that GHSR is characterized by a specific hydration pattern that is selectively remodeled by pharmacologically distinct ligands and by the lipid environment. This process is directly related to the concerted movements of the transmembrane domains of the receptor. These results demonstrate that the conformational dynamics of GHSR are tightly coupled to the movements of internal water molecules, further enhancing our understanding of the molecular bases of GPCR-mediated signaling.

    View details for DOI 10.7554/eLife.63201

    View details for Web of Science ID 000693090200001

    View details for PubMedID 34477105

    View details for PubMedCentralID PMC8416020

  • Structure of the agonist 12-HHT in its BLT2 receptor-bound state. Scientific reports Giusti, F., Casiraghi, M., Point, E., Damian, M., Rieger, J., Bon, C. L., Pozza, A., Moncoq, K., Baneres, J., Catoire, L. J. 2020; 10 (1): 2630

    Abstract

    G Protein-Coupled receptors represent the main communicating pathway for signals from the outside to the inside of most of eukaryotic cells. They define the largest family of integral membrane receptors at the surface of the cells and constitute the main target of the current drugs on the market. The low affinity leukotriene receptor BLT2 is a receptor involved in pro- and anti-inflammatory pathways and can be activated by various unsaturated fatty acid compounds. We present here the NMR structure of the agonist 12-HHT in its BLT2-bound state and a model of interaction of the ligand with the receptor based on a conformational homology modeling associated with docking simulations. Put into perspective with the data obtained with leukotriene B4, our results illuminate the ligand selectivity of BLT2 and may help define new molecules to modulate the activity of this receptor.

    View details for DOI 10.1038/s41598-020-59571-6

    View details for PubMedID 32060341

  • NMR analysis of GPCR conformational landscapes and dynamics MOLECULAR AND CELLULAR ENDOCRINOLOGY Casiraghi, M., Point, E., Pozza, A., Moncoq, K., Baneres, J., Catoire, L. J. 2019; 484: 69–77

    Abstract

    Understanding the signal transduction mechanism mediated by the G Protein-Coupled Receptors (GPCRs) in eukaryote cells represents one of the main issues in modern biology. At the molecular level, various biophysical approaches have provided important insights on the functional plasticity of these complex allosteric machines. In this context, X-ray crystal structures published during the last decade represent a major breakthrough in GPCR structural biology, delivering important information on the activation process of these receptors through the description of the three-dimensional organization of their active and inactive states. In complement to crystals and cryo-electronic microscopy structures, information on the probability of existence of different GPCR conformations and the dynamic barriers separating those structural sub-states is required to better understand GPCR function. Among the panel of techniques available, nuclear magnetic resonance (NMR) spectroscopy represents a powerful tool to characterize both conformational landscapes and dynamics. Here, we will outline the potential of NMR to address such biological questions, and we will illustrate the functional insights that NMR has brought in the field of GPCRs in the recent years.

    View details for DOI 10.1016/j.mce.2018.12.019

    View details for Web of Science ID 000457872600008

    View details for PubMedID 30690069