Mike Lawrence


Walter and Eliza Hall Institute of Medical Research

Associate Professor Mike Lawrence

I began my research career in 1978, undertaking a PhD degree in theoretical physics at the University of Cape Town (UCT) in South Africa. My thesis concerned the semi-classical modelling of the quantum mechanics of protein tunnelling in hydrogen-bonded compounds, and it was heavily based on my mathematics and physics background. However, I was always fascinated by the application of these disciplines to the life sciences and in 1980, I was fortunate to secure funds for a two-year postdoc at the MRC Laboratory for Molecular Biology in Cambridge, UK. This was a turning point in my career and I found myself on a very steep learning curve! During the postdoc I determined the structure of the T-state of the allosteric enzyme phosphofructokinase from Bacillus stearothermophilus and developed techniques in electron micrograph image alignment, some of which are still used today in cryo-tomography.

I then returned to South Africa for five years. Unfortunately, South Africa had no resources at the time for structural biology, but nevertheless I secured the directorship of a small electron microscopy facility within the science faculty at UCT and had quite a bit of fun.

In 1988, I emigrated to Australia and joined the research group headed by Peter Colman, which proved to be a further turning point of my career. During my eighteen years at CSIRO, I worked on a number of particularly challenging projects in structural biology, including determination of the structure of phaseolin (a seed storage protein), the fusion protein of Newcastle disease virus (NDV-F) and, ultimately, the extracellular domain of the human insulin receptor, in a project led by Dr Colin Ward. The insulin receptor project terminated in 2006 and I decided to accept a position as a laboratory head at the Walter and Eliza Hall Institute of Medical Research (WEHI) in Parkville, Victoria, to continue the quest to determine how insulin bound to and activated its receptor. This opportunity was undoubtedly the most exciting in my career, not only because it offered me significant independence but also because it gave me the opportunity to pursue a very important and still unsolved problem in structural biology, with direct application to human health. The WEHI has proved to be an incredibly supportive and stimulating environment in which to work. In 2013, my lab finally obtained the first atomic picture of insulin bound to its receptor and published it in Nature. Since then my laboratory has sought to build on this finding, not only to fill in the many gaps remaining but to pursue active ways of translating it into better insulins and into applications in cancer.