The Institute of Cancer and Genomic Sciences recently appointed Steve Smerdon as Professor of Structural Biology. He joins the University of Birmingham from The Francis Crick Institute, London.
For me, the interests, expertise and excellence of the research groups in the DNA-damage area within the Institute of Cancer and Genomic Sciences at Birmingham have been a major attraction and co-location presents exciting opportunities to develop collaborations in areas both related to my existing interests and beyond. As importantly, I have been impressed by a real enthusiasm at the University for structural biology that is clearly driven by an appreciation of its value and significance for modern, integrated approaches to biomedical research.
Although I have focussed mainly on structural analysis of human DNA-damage response pathways for many years, my interests have been somewhat broader ranging from kinetic barriers to ligand binding as a PhD student, through mechanisms of reverse transcription as a post-doc and subsequently, a number of signalling systems that variously regulate the cell-cycle, cytoskeletal organisation and bacterial pathogenesis.
Much of our work has been, and continues to be, multi-disciplinary involving contributions from different areas of expertise ranging from molecular and cell biology, biochemistry and chemical biology to crystallography, nuclear magnetic resonance, biophysical analysis, mass spectrometry and, most recently, electron microscopy.
As part of the Institute of Cancer and Genomic Sciences, I hope to be able to continue our efforts to unpick the molecular complexities of DNA-damage signalling and, of course, to explore new areas of common interest with the existing groups. As a natural extension of these interactions, I am also keen to provide the opportunity for other labs to incorporate structural and biophysical techniques into their experimental ‘arsenal’.
Of course, these are particularly exciting times in structural research with developments in electron microscopy already proving to be transformative and a major goal will certainly be to help the University realise it’s aspirations for future developments in this important area.
From a research perspective, I guess the most significant achievement has been to show that the regulation of protein-protein interactions constitutes one of the major functional roles of protein phosphorylation in living cells. The recognition of a phosphate group would seem to be a straightforward task. However, our work has rather shown a surprising diversity associated with these molecular recognition processes and this has, in turn, contributed to the understanding of specificity and control of macromolecular assembly in many different signalling contexts.
The answer to this is a rather simple one. Structural biology and particularly my own area of interest, X-ray crystallography, can provide unparalleled insights into molecular mechanisms. To understand biological function at the molecular level is immensely rewarding and the joy and privilege of seeing a new structure in all of its atomic detail is the same now as it was when I first started as a PhD student 30 years ago!