Miss Rekia Berrahmouni

Research project: Inverse agonism at the Beta 3 adrenoceptor


Beta adrenergic receptors or ?-adrenoceptors are G-protein coupled receptors (GPCR) consisting of seven transmembrane alpha helix domains. These domains have an extracellular N terminus displaying an amine group and also an intracellular C terminus exposing a carboxylic acid group. Also attached to the seven domains, is a heterotrimeric G-protein composed of three subunits: alpha, beta and gamma. GPCRs are metabotropic receptors that use ligands to carry a signal from the extracellular environment to the intracellular space via second messengers. Both b1 and b2 adrenoceptors have been shown to be predominately Gs coupled, meaning they work via adenylate cyclase (AC) as the second messenger. Upon a ligand binding to a b1 or b2 adrenoceptor, a conformational change occurs in the 7 transmembrane structure resulting in the dissociation of the G- protein. When inactive, the alpha subunit of the G-protein is bound to a GDP (guanosine diphosphate) molecule. Upon activation, the GDP is exchanged for GTP (guanosine triphosphate) which has a higher affinity for AC. The alpha subunit with bound GTP dissociates from the rest of the G-protein and binds to AC. This activates AC which in turn converts adenosine triphosphate (ATP) to cAMP. cAMP then binds to the regulatory subunit of protein kinase A (PKA), liberating it from the catalytic subunit which is then ready to phosphorylate proteins (such as calcium channels) within the cell. 


Studying a Bsc in Pharmaceutical Science allowed mento explore various pathways. Undertaking a biology based module in my final year caught my attention to explore this in a Masters in Research. By achieving this masters I would like to explore more into how the pharmaceutical research is obtained.


  • BSc Pharmaceutical Science