I am interested in the function (and disfunction) of membrane proteins in disease. During my PhD at the MRC LMB in Cambridge under Chris Tate, I attempted to solve the structure of a bacterial drug resistance transporter with the aid of stabilising mutations. After this, I joined an industrial postdoctoral scheme working on a malarial drug resistance transporter. In my current postdoctoral position at the University of Leeds, I have drawn on my expertise in membrane protein purification and analysis to study ion channels involved in cardiovascular diseases. In previous work, x-ray crystallography was the technique of choice for structure determination; however now we aim to use cryoEM to determine these ion channel structures. Potent activators and inhibitors of our target ion channels have been discovered; however these are not suitable drug candidates. For this reason we are also attempting to use crosslinking to find out where these molecules bind to the channel so that we may design future drugs with more suitable properties. Additionally, I have a keen interest in new technologies and in particular how to use them to study challenging membrane proteins in as close to native conditions as possible.
Shake-it-off: A simple ultrasonic cryo-EM specimen preparation device
David Wright
Microfluidic protein isolation and sample preparation for high resolution cryo-EM
David Wright
Structures of the Otopetrin Proton Channels Otop1 and Otop3
David Wright
Retrieving High-Resolution Information from Disordered 2D Crystals by Single Particle Cryo-EM
David Wright
The structural basis for release factor activation during translation termination revealed by time-resolved cryogenic electron microscopy
David Wright