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Click here to search FindAPhD.com for PhD studentship opportunities(BBSRC CASE) Investigating the structure and dynamics of G protein-coupled receptors by EPR Spectroscopy and other cutting-edge methodologies
About the Project
Membrane proteins (MPs) make up a significant part of the genome and are the target of ~30% of therapeutics and yet our structural and functional understanding often lags behind their soluble counterparts. G protein-coupled receptors (GPCRs) are the largest family of membrane proteins and mediate most of physiological responses to hormones and environmental stimulants and are responsible for olfaction, vision and taste. GPCRs account for 50% of all MP targets and are expressed ubiquitously in humans. Exciting new developments in Structural EPR spectroscopy, which allows for accurate distance measurements between spin pairs introduced on selected protein sites, have changed the way we can study membrane protein structure and provide new insights into our fundamental understanding in their dynamics to drive therapeutic design. This project will combine advanced structural EPR spectroscopy, complemented by Mass spectrometry and CryoEM to probe GPCR dynamics, using a variety of cutting edge techniques and make use of the new BioEmPiRe centre, in addition to collaborating with the National Research Facility for EPR in Manchester. Work will focus on Cannabinoid 1 (CB1) receptor, which is mainly expressed in the brain and is responsible for many of the psychoactive effects of cannabinoids and Cannabinoid 2 (CB2) receptor, which has a more localised distribution, being expressed in several immune cells and neurones. By understanding the role of receptor dynamics on GPCR activation and ligand activity, we are aiming to provide new insights into small molecule drug action mechanism that could be used to develop novel more efficacious drugs. The successful PhD student will be trained in complementary cutting edge techniques of interest to both academia and the collaborating company Z7 Biotech Ltd, our industrial partner in this project.
Relevant links
Pliotas Group Website: https://www.pliotasgroup.org/
UoM Research Profile: https://research.manchester.ac.uk/en/persons/christos-pliotas
X: @PliotasGroup
Dr Argyris Politis: https://research.manchester.ac.uk/en/persons/argyris.politis
Dr Alice Bowen: https://research.manchester.ac.uk/en/persons/alice.bowen
Eligibility
Applicants must have obtained or be about to obtain a First or Upper Second class UK honours degree, or the equivalent qualifications gained outside the UK, in an appropriate area of science, engineering or technology.
Before you Apply
Applicants must make direct contact with preferred supervisors before applying. It is your responsibility to make arrangements to meet with potential supervisors, prior to submitting a formal online application.
How To Apply
To be considered for this project you MUST submit a formal online application form - full details on eligibility how to apply can be found on the BBSRC DTP website https://www.bmh.manchester.ac.uk/study/research/funded-programmes/bbsrc-dtp/
Your application form must be accompanied by a number of supporting documents by the advertised deadlines. Without all the required documents submitted at the time of application, your application will not be processed and we cannot accept responsibility for late or missed deadlines. Incomplete applications will not be considered. If you have any queries regarding making an application please contact our admissions team [Email Address Removed]
Equality, Diversity and Inclusion
Equality, diversity and inclusion is fundamental to the success of The University of Manchester, and is at the heart of all of our activities. The full Equality, diversity and inclusion statement can be found on the website https://www.bmh.manchester.ac.uk/study/research/apply/equality-diversity-inclusion/
Funding Notes
References
2. Haysom SF, Machin J, Whitehouse JM, Horne JE, Fenn K, Ma Y, El Mkami H, Böhringer N, Schäberle TF, Ranson NA, Radford SE, Pliotas C. Darobactin B Stabilises a Lateral-closed conformation of the BAM Complex in E. coli cells. Angewandte Chemie International Edition, 62, 34, e202218783, 2023
3. Wang B, Lane BJ, Kapsalis C, Ault JR, Sobott F, El Mkami H, Calabrese AN, Kalli AC, Pliotas C. Pocket delipidation induced by membrane tension or modification leads to a structurally analogous mechanosensitive channel state. Structure 30, 1-15, 2022
4. Kapsalis C, Wang B, El Mkami H, Pitt SJ, Schnell JR, Smith TK, Lippiat JD, Bode BE, Pliotas C. Allosteric activation of an ion channel triggered by modification of mechanosensitive nano-pockets. Nature Communications 10, 4619, 2019
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