Claudia Stohrer, ESR3

picture claudia rognee

Claudia works at the Unviersity of Leeds, UK.

Her PhD subject is Structure determination of the Adenosine receptor A2A in complex with intracellular binding partners.

On Twitter: @ClaudiaStohrer

Tell us about yourself

I grew up in Switzerland near the city of Basel. Biology was always my favourite subject, and during high school I could follow up my interests. With “Schweizer Jugend Forscht”, I got my first opportunity to get to know research work at University level by carrying out a little research project at the University of Geneva. I absolutely loved it! Following this experience I decided to study molecular Biology at the University of Basel. My interests during my undergraduate focused on the processes happening inside a single cell, so I continued with a Masters in Molecular Biology with a major in cell biology and Biochemistry. For my Master’s Thesis I investigated the trafficking of a membrane protein from the Trans-Golgi network to the plasma membrane. After finishing my Master’s I went to Novartis for an internship, to learn how research is carried out in industry. It was during that internship that I got more interested in structure biology and also got introduced to the world of GPCRs, the topic of my current PhD.

If I’m not in the lab, I like to spend time at the pool, either working as a swimming instructor for kids or as a lifesaving swimmer. I also enjoy music a lot by playing in an orchestra and dancing.

Why are you interested in science?

My mom is a medical doctor and my dad is an engineer, so I grew up in a science encouraging environment. I was always curious and wanted to understand how things work. Following my mother’s example already as a little girl I wanted to become a doctor. For me this profession contained the perfect combination of social interaction and the opportunity to study biological processes. However, I realised that the more I learned about science, and especially biology, the more I wanted to know about all the molecular details. To satisfy this desire of going more into depth, I became a scientist and not a physician.

Please tell us about your PhD project:

G protein-couple receptors (GPCRs) are membrane receptors which translate a signal from the outside of the cell to the inside. This signal can be almost anything, reaching from light and hormones to small chemical compounds. When the signal arrives at the receptor it introduces some structural changes (makes the receptor change its shape) which leads to the activation of the so-called G Protein on the inside of the receptor. This can then activate a variety of different signalling pathways inside the cell.

They are involved in almost all physiological processes and therefore represent interesting drug targets. About 30% of the drugs marketed today are targeting GPCRs!

To be able to understand how this signal is translated from the outside into the inside of the cell and to the intracellular signalling partners we need to know more about their 3D structure. This can be investigated by X-ray crystallography. GPCRs are however very hard to crystallise. Only in the last years and with the help of another technique called cryo-electron microscopy it was possible to look at some first GPCRs in complex with the G Protein.

However, GPCRs do not only interact with the G Protein, but also with many other proteins. In my PhD I am working with the Adenosine receptor. This receptor is required to keep your heart from speeding up too much and is also the reason why coffee keeps you awake. For this receptor several interaction partners have been identified; we however do not exactly know how they interact. I want to generate a complex of the Adenosine receptor and some of these interaction partners, which I then will try to crystallise to see with X-ray crystallography how they interact.

What do you or did you enjoy most until now in your position within RAM network? Why?

While I was on my first secondment in Hamburg we had some high school students visiting for two mornings to whom we showed the beam line they have there. The students were blown away by all the equipment and robots there, as was I. One of the students asked if we understand everything in there. Of course not! There is a specialist taking care of the robotics, one for the software, another one for the beams and again somebody else who knows about the samples. And that’s exactly the great beauty about science and especially our program: You do not need to know everything, but you collaborate with people specialized in other areas and together you are able to put the pieces together and reveal novel insights. I think it is an amazing opportunity to be in a network with people from different disciplines working together on the same goal: rationalising membrane protein crystallisation!

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