Research groups

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Research

Living Molecules-Biomolecular Structures

Crystal structures of (a, left) a synthetic protein forming a channel, and (b) ECM-interacting head domain of a bacterial adhesin, UspA1.

The vast majority of life processes result from the binding of a protein to another molecule. Understanding these interactions at the molecular level is the key to life itself, and provides invaluable insight for the treatment of diseases.

Through the study of protein structure, primarily using protein crystallography, we aim to probe crucial biomolecular interactions central to a variety of diseases. The aim is very much to use this information to accelerate the development of new drugs and therapeutics.

Studies within the group focus on a variety of proteins including cell surface receptors, metabolic enzymes involved in diseases such as malaria and cancer, and designer proteins as building blocks in synthetic biology. Our work is characterised by an interdisciplinary approach to biological function and we typically employ a wide range of techniques from recombinant DNA technology, protein purification and characterisation, proteomics approaches through to structure determination using crystallography, AFM, EM and SAXS, and molecular modelling.

Group

Chris Agnew, Ming Attarataya, Richard Birkinshaw, Nick Burton, Rebecca Conners, and Nathan Zaccai.

Recent publications

Zaccai NR, Chi B, Thomson AR, Boyle AL, Bartlett GJ, Bruning M, Linden N, Sessions RB, Booth PJ, Brady RL, Woolfson DN. (2011) A de novo peptide hexamer with a mutable channel. Nature Chemical Biology. 7: 935-941.

Agnew C, Borodina E, Zaccai NR, Conners R, Burton NM, Vicary JA, Cole DK, Antognozzi M, Virji M, Brady RL. (2011) Correlation of in situ mechanosensitive responses of the Moraxella catarrhalis adhesin UspA1 with fibronectin and receptor CEACAM1 binding. PNAS (USA). 108(37): 15174-15178.

Singleton BK, Lau W, Fairweather VS, Burton NM, Wilson MC, Parsons SF, Richardson BM, Trakarnsanga K, Brady RL, Anstee DJ, Frayne J. (2011) Mutations in the second zinc finger of human EKLF reduce promoter affinity but give rise to benign and disease phenotypes. Blood. 118(11): 3137-3145.

Conners R, Hill DJ, Borodina E, Agnew C, Daniell SJ, Burton NM, Sessions RB, Clarke AR, Catto LE, Lammie D, Wess T, Brady RL, Virji M. (2008) The Moraxella adhesin UspA1 binds to its human CEACAM1 receptor by a deformable trimeric coiled-coil. EMBO Journal. 27(12): 1779-1789.

View all publications listed on the University of Bristol's publication database