Faculty of Biological Sciences

Dr Dan Donnelly

BSc, Leicester; PhD 1992, London.
Senior Lecturer
School of Biomedical Sciences

Contact:  Garstang 6.41d | +44(0) 113 34 37761 | email address for  

Research Interests

G Protein-Coupled Receptor - structure and function.

 

GLP-1, PTH and CGRP receptors

 

Current Projects

The laboratory studies the structure & function of G protein-coupled receptors - one of the most diverse and ubiquitous families of integral membrane proteins. GPCRs play a pivotal role in many cellular signalling pathways and are prime targets for the development of therapeutic agents designed to either block or activate the receptors. The aim of this laboratory is to elucidate the mechanism by which these receptors bind their ligands and transduce the signal across the plasma membrane. The research in my lab concentrates primarily on the glucagon-like peptide-1 (GLP-1) receptor (funded by BBSRC & AstraZeneca; previous funding has come from Novo Nordisk, The Royal Society, BBSRC and Diabetes UK) and the parathyroid hormone and CRLR receptors (funding from GSK & BBSRC).

 

Faculty Research and Innovation


Studentship information

Undergraduate project topics:

  • G Protein-Coupled Receptor - structure and function.

Postgraduate studentship areas:

  • The Structure and Function of the 7TM Receptor for Glucagon-like Peptide-1 (GLP-1)

See also:

Admin roles

FBS FTSEC
FBS UGTSEC
Library Representative
UG Programme Leader: Pharmacology

Modules managed

BMSC2224 - Principles of Drug Discovery
BMSC3143 - Advanced Topics in Pharmacology I
BMSC3233 - Advanced Topics in Pharmacology II

Modules taught

BIOC3221/22/23/BIOL3210/BMSC3233/34/35/36 - ATU 23 - Membrane proteins
BMSC1212 - Introduction to Pharmacology
BMSC1213 - Basic Laboratory and Scientific Skills 2
BMSC2119 - Experimental Skills
BMSC2119/3302 - Experimental Skills/Medical Pharmacology
BMSC2224 - Principles of Drug Discovery
BMSC2230 - Topics in Pharmacology
BMSC3143 - Advanced Topics in Pharmacology I
BMSC3143/44/45/46 - ATUs - BMS specific
BMSC3301 - Research Proj: Biomed Sciences

Committees

Member of Undergraduate School Taught Student Education Committee

Group Leader Dr Dan Donnelly  (Senior Lecturer)

G Protein-Coupled Receptor - structure and function. 


Ravichandran S; Singh N; Donnelly D; Migliore M; Johnson P; Fishwick C; Luke BT; Martin B; Maudsley S; Fugmann SD; Moaddel R Pharmacophore model of the quercetin binding site of the SIRT6 protein. J Mol Graph Model 49 38-46, 2014
DOI:10.1016/j.jmgm.2014.01.004
View abstract

Donnelly D The structure and function of the glucagon-like peptide-1 receptor and its ligands. Br J Pharmacol 166 27-41, 2012
DOI:10.1111/j.1476-5381.2011.01687.x
View abstract

Barwell J; Miller PS; Donnelly D; Poyner DR Mapping interaction sites within the N-terminus of the calcitonin gene-related peptide receptor; the role of residues 23-60 of the calcitonin receptor-like receptor PEPTIDES 31 170-176, 2010
DOI:10.1016/j.peptides.2009.10.021

Mann RJ; Nasr NE; Sinfield JK; Paci E; Donnelly D The major determinant of exendin-4/glucagon-like peptide 1 differential affinity at the rat glucagon-like peptide 1 receptor N-terminal domain is a hydrogen bond from SER-32 of exendin-4 BRIT J PHARMACOL 160 1973-1984, 2010
DOI:10.1111/j.1476-5381.2010.00834.x

Chapman KL; Kinsella GK; Cox A; Donnelly D; Findlay JBC Interactions of the Melanocortin-4 Receptor with the Peptide Agonist NDP-MSH J MOL BIOL 401 433-450, 2010
DOI:10.1016/j.jmb.2010.06.028

Miller PS; Barwell J; Poyner DR; Wigglesworth MJ; Garland SL; Donnelly D Non-peptidic antagonists of the CGRP receptor, BIBN4096BS and MK-0974, interact with the calcitonin receptor-like receptor via methionine-42 and RAMP1 via tryptophan-74 BIOCHEM BIOPH RES CO 391 437-442, 2010
DOI:10.1016/j.bbrc.2009.11.076

Mann RJ; Al-Sabah S; de Maturana RL; Sinfield JK; Donnelly D Functional coupling of Cys-226 and Cys-296 in the glucagon-like peptide-1 (GLP-1) receptor indicates a disulfide bond that is close to the activation pocket PEPTIDES 31 2289-2293, 2010
DOI:10.1016/j.peptides.2010.09.015

Mann R; Wigglesworth MJ; Donnelly D Ligand-receptor interactions at the parathyroid hormone receptors: Subtype binding selectivity is mediated via an interaction between residue 23 on the ligand and residue 41 on the receptor MOL PHARMACOL 74 605-613, 2008
DOI:10.1124/mol.108.048017

Weaver RE; Donnelly D; Wabitsch M; Grant PJ; Balmforth AJ Functional expression of glucose-dependent insulinotropic polypeptide receptors is coupled to differentiation in a human adipocyte model INT J OBESITY 32 1705-1711, 2008
DOI:10.1038/ijo.2008.148

Mann R; Nasr N; Hadden D; Sinfield J; Abidi F; Al-Sabah S; de Maturana RL; Treece-Birch J; Willshaw A; Donnelly D Peptide binding at the GLP-1 receptor BIOCHEM SOC T 35 713-716, 2007

Ellis J; Warburton P; Donnelly D; Balmforth AJ Conformational induction is the key process for activation of the AT(1) receptor BIOCHEM PHARMACOL 71 464-471, 2006
DOI:10.1016/j.bcp.2005.11.011

Cox A; Donnelly D; Kaur M; Cheetham SC; Cockcroft VB; Findlay JBC MTSEA prevents ligand binding to the human melanocortin-4 receptor by modification of cysteine 130 in transmembrane helix 3 FEBS LETT 579 285-291, 2005
DOI:10.1016/j.febslet.2004.11.087

de Maturana RL; Treece-Birch J; Abidi F; Findlay JBC; Donnelly D Met-204 and Tyr-205 are together important for binding GLP-1 receptor agonists but not their N-terminally truncated analogues PROTEIN PEPTIDE LETT 11 15-22, 2004

Al-Sabah S; Donnelly D The primary ligand-binding interaction at the GLP-1 receptor is via the putative helix of the peptide agonists PROTEIN PEPTIDE LETT 11 9-14, 2004

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 BRIT J PHARMACOL 140 339-346, 2003
DOI:10.1038/sj.bjp.0705453

de Maturana RL; Willshaw A; Kuntzsch A; Rudolph R; Donnelly D The isolated N-terminal domain of the glucagon-like peptide-1 (GLP-1) receptor binds exendin peptides with much higher affinity than GLP-1 J BIOL CHEM 278 10195-10200, 2003
DOI:10.1074/jbc.M212147200

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 LETT 553 342-346, 2003
DOI:10.1016/S0014-5793(03)01043-3

López de Maturana R; Donnelly D The glucagon-like peptide-1 receptor binding site for the N-terminus of GLP-1 requires polarity at Asp198 rather than negative charge. FEBS Lett 530 244-248, 2002
View abstract

de Maturana RL; Donnelly D The glucagon-like peptide-1 receptor binding site for the N-terminus of GLP-1 requires polarity at Asp198 rather than negative charge (FEBS 26658) (vol 530, pg 244, 2002) FEBS LETT 531 572-572, 2002

López de Maturana R; Donnelly D Erratum: The glucagon-like peptide-1 receptor binding site for the N-terminus of GLP-1 requires polarity at Asp198 rather than negative charge (FEBS Letters (2002) 530 (244-248) PII: S0014579302034920) FEBS Letters 531 572-572, 2002
DOI:10.1016/S0014-5793(02)03619-0

Donnelly D; Maudsley S; Moser RN; Hurrell CR; Gent JP; Findlay JBC Conserved polar residues in the transmembrane domain of the human tachykinin NK2 receptor: functional roles and structural implications. Biochemical Journal 339 56-61, 1999

Maudsley S; Gent JP; Findlay JBC; Donnelly D The relationship between the agonist-induced activation and desensitisation of the human tachykinin NK2 receptor expressed in Xenopus oocytes. British Journal of Pharmacology 124 675-684, 1998

Balmforth AJ; Lee AJ; Warburton P; Donnelly D; Ball SG The specificity of Peptide-Binding of the Angiotensin AT1 receptor is Dependent on an Interaction Between Transmembrane Helices III and VII Journal of Biological Chemistry 272 4245-4251, 1997

Balmforth AJ; Lee AJ; Shepherd FH; Warburton P; Donnelly D; Ball SG G-protein-coupled receptors for peptide hormones: angiotensin II receptors. Biochemical Society Transactions 25 1041-1046, 1997

Donnelly D The arrangement of the transmembrane helices in the secretin receptor family of G protein-coupled receptors FEBS Letters 409 431-436, 1997
View abstract