Membrane Protein Structure and Function

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Group leader: Dr Alex Conner


We use molecular and cellular techniques to understand the structure, activation and localisation of large transmembrane proteins. We have identified novel activation mechanisms for the cardiovascular calcitonin gene-related peptide (CGRP) receptor and discovered a new trigger for cellular trafficking of the aquaporin (AQP) family of water pores.

Our research group

We are interested in understanding the docking of ligands and activation of the second largest family of G protein-coupled receptors (GPCRs). We use site-directed mutagenesis to identify key areas of functional importance with focus on the potent vasodilator calcitonin gene-related peptide (CGRP) and its receptor. We compare receptors though ligand binding, cell-surface expression, second messenger activation and agonist-mediated internalisation/desensitisation.

We use similar techniques to understand the sub-cellular relocalisation of the water channel transmembrane proteins (aquaporins; AQPs). This is important for a number of processes in health and disease including kidney function, stroke and trauma.

Current Projects

  • Understanding the second extracellular loop of the calcitonin gene-related peptide receptor
  • Docking calcitonin gene-related peptide into its receptor as a platform for cardiovascular drug design
  • The effect of hypotonicity changes to aquaporin sub-cellular reorganisation (aquaporin 1and 4)
  • Oligomerisation of Aquaporin 4; a functional role
  • The physiological significance of aquaporin 4 in astrocytes as a model of cytotoxic oedema

Recent Publications

For full publication list see:


Principal Investigators
Dr Alex Conner

PhD Students
Mr Philip Kitchen
Mr Luke Taylor
Mr Mike Woolley