DPhil, Chemistry. University of York, 1993 BSc Biophysics. University of Leeds 1989

Almost 30 % of all genomes sequenced to date encode membrane proteins. These play vital roles in many areas of cell biology such as signalling, the selective uptake or removal of molecules from the cell and the maintenance of cellular pH or ion concentration. Despite their importance in physiology and drug discovery there is a relative paucity in the number of structures solved. The goal of my research is in understanding the structure and mechanism of these dynamic proteins through the use of X-ray crystallography in combination with other biochemical and biophysical techniques.

In particular my group is focussed on secondary active transporters. These proteins harness electrochemical gradients to transport ions or molecules across membranes. We have solved the structure of a number of transporters and are probing their mechanisms through a combination of X-ray crystallography, biochemistry, site-directed mutagenesis, chemistry and computational chemistry.

Coincon, Mathieu, Uzdavinys, Povilas, Nji, Emmanuel, Dotson, David L., Winkelmann, Iven, Abdul-Hussein, Saba, Cameron, Alexander, Beckstein, Oliver, Drew, David. 2016. Crystal structures reveal the molecular basis of ion translocation in sodium/proton antiporters. Nature Structural & Molecular Biology, 23 (3), pp. 248-255, View Alguel, Yilmaz, Amillis, Sotiris, Leung, James, Lambrinidis, George, Capaldi, Stefano, Scull, Nicola J., Craven, Gregory, Iwata, So, Armstrong, Alan, Mikros, Emmanuel, Diallinas, George, Cameron, Alexander, Byrne, Bernadette. 2016. Structure of eukaryotic purine/H+ symporter UapA suggests a role for homodimerization in transport activity. Nature Communications, 7, pp. 1-9, View Arakawa, Takatoshi, Kobayashi-Yurugi, Takami, Alguel, Yilmaz, Iwanari, Hiroko, Hatae, Hinako, Iwata, Momi, Abe, Yoshito, Hino, Tomoya, Ikeda-Suno, Chiyo, Kuma, Hiroyuki, Kang, Dongchon, Murata, Takeshi, Hamakubo, Takao, Cameron, Alexander, Kobayashi, Takuya, Hamasaki, Naotaka, Iwata, So. 2015. Crystal structure of the anion exchanger domain of human erythrocyte band 3. Science, 350 (6261), pp. 680-684, View Lee, Chiara, Yashiro, Shoko, Dotson, David L., Uzdavinys, Povilas, Iwata, So, Sansom, Mark S. P., von Ballmoos, Christoph, Beckstein, Oliver, Drew, David, Cameron, Alexander. 2014. Crystal structure of the sodium-proton antiporter NhaA dimer and new mechanistic insights. The Journal of General Physiology, Volume 144 (Number 6), pp. 529-544, View Simmons, Katie J., Jackson, Scott M., Brueckner, Florian, Patching, Simon G., Beckstein, Oliver, Ivanova, Ekaterina, Geng, Tian, Weyand, Simone, Drew, David, Lanigan, Joseph, Sharples, David J., Sansom, M. S. P. (Mark S. P.), Iwata, So, Fishwick, Colin W. G., Johnson, A. Peter, Cameron, Alexander, Henderson, P. J. F. (Peter J. F.). 2014. Molecular mechanism of ligand recognition by membrane transport protein, Mhp1. The EMBO Journal, 33 (16), pp. 1831-1844, View Lee, Chiara, Kang, Hae Joo, von Ballmoos, Christoph, Newstead, Simon, Uzdavinys, Povilas, Dotson, David L., Iwata, So, Beckstein, Oliver, Cameron, Alexander, Drew, David. 2013. A two-domain elevator mechanism for sodium/proton antiport. Nature, Volume 501 (Number 7468), pp. 573-577, View Foadi, James, Aller, Pierre, Alguel, Yilmaz, Cameron, Alexander, Axford, Danny, Owen, Robin L., Armour, Wes, Waterman, David G., Iwata, So, Evans, Gwyndaf. 2013. Clustering procedures for the optimal selection of data sets from multiple crystals in macromolecular crystallography. Acta Crystallographica Section D Biological Crystallography, Volume 69 (Number 8), pp. 1617-1632, View