About the Project
My lab's interest is in the structure & function of Family B G protein-coupled receptors. Current projects include studies by 2 post docs and 3 PhD students on the GLP-1 receptor, PTH-1 and PTH-2 receptors and the Calcitonin/CGRP receptors - these projects are funded by BBSRC, GSK and AstraZeneca.
Residues of the GPCR that are potentially involved in ligand binding will be targeted for mutagenesis. The mutant receptors will then be expressed in mammalian cell lines and analysed via ligand binding and cAMP assays so that the nature of the binding site can be better understood. The outcomes will be visualised using molecular modelling.
Funding Notes
Applications are welcome at any time, but deadlines exist for some awards (see http://www.fbs.leeds.ac.uk/gradschool/research/PhDStudentships.htm). Offers are made to the most able students as soon as possible.
References
Some papers in this research area that were published by PhD students in my lab:
Al-Sabah, S.; Donnelly, D., The positive charge at Lys-288 of the glucagon-like peptide-1 (GLP-1) receptor is important for binding the N-terminus of peptide agonists FEBS Letters, 533, pp.342-346, 2003
Al-Sabah, S.; Donnelly, D., A model for receptor-peptide binding at the glucagon-like peptide-1 (GLP-1) receptor through the analysis of truncated ligands and receptors British Journal of Pharmacology, 140, pp.339-346, 2003
Lopez de Maturana, R.; Willshaw, A.; Kuntzsch, A.; Rudolph, R.; Donnelly, D., The isolated N-terminal domain of the glucagon-like peptide-1 receptor binds exendin peptides with much higher affinity that GLP-1 Journal of Biological Chemistry, 278, pp.10195-10200, 2003
Lopez de Maturana R.; Donnelly, D., The glucagon-like peptide - 1 receptor binding site for the N-terminus of GLP - 1 requires polarity at Asp 198 rather than negative charge. F E B S Letters, 530, pp.244-248, 2002
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