Department of Biochemistry University of Oxford Department of Biochemistry
University of Oxford
South Parks Road
Oxford OX1 3QU

Tel: +44 (0)1865 613200
Fax: +44 (0)1865 613201
Collage of Drosophila third instar larva optic lobe
Lu Yang, Davis lab
First year Biochemistry students at a practical class
Image showing the global movement of lipids in a model planar membrane
Matthieu Chavent, Sansom lab
Anaphase bridges in fission yeast cells
Whitby lab
Lactose permease represented using bending cylinders in Bendix software
Caroline Dahl, Sansom lab
Epithelial cells in C. elegans showing a seam cell that failed to undergo cytokinesis
Serena Ding, Woollard lab
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UNESCO/ L'Oreal Rising Talent Award won by graduate student alumna
Areej Abuhammad Areej Abuhammad, who started her career as a graduate student (2009-2013) working jointly in the Biochemistry and Pharmacology Departments, has won a 2018 UNESCO/L'Oreal Rising Talent Award Published: 19 March 2018
Antisense transcription influences sense transcription
Antisense transcription affects the rate of transcription initiation and nuclear processing of RNA through histone acetylation levels New research by the Mellor and Angel groups, published in Molecular Systems Biology, provides new insights into the biological function of antisense transcription. The results highlight a role of antisense transcription in influencing the production of sense transcripts, ultimately determining the levels of functional protein Published: 19 March 2018
Mechanism of cationic amino acid transport revealed in new crystal structure
Structure of GkApcT with the predicted gating helices shown. Movement of TM6 away from TM3 and 8 opens the binding site to the interior of the cell, and facilitates release of the bound amino acid New research by the Newstead group, published in Nature Communications, reveals the first crystal structure for a bacterial homologue of the mammalian cationic amino acid transporters GkApcT providing insight into amino acid selectivity and transport mechanism in this physiologically important transporter family Published: 27 February 2018
A new class of ion pump inhibitors could help fight infectious fungi
Cartoon representation of the Ca2+-pump bound to a HyC (labeled 7). Pump domains and ligands are indicated. The bound HyC and ATP analogue TNPATP are shown as sticks (C: yellow or marine, O: red, Br: dark red, F: pale cyan, N: blue, P: orange) B) Sliced surface view revealing the the ligand-binding pocket at the membrane interface New research by the Bublitz group in collaboration with the Danish drug discovery company PCovery, describes a new class of compounds that inhibit the growth of fungal cells by disrupting their plasma membrane potential Published: 27 February 2018

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Mark Sansom, Head of Department

The Department of Biochemistry at the University of Oxford is a centre for world class research and teaching of all aspects of Biochemistry by staff from many different backgrounds and nationalities. Our research addresses a wide range of questions relating to the fundamental basis of all cellular life from man to microbes. This work explains the structures and functions of proteins and nucleic acids, and in doing so addresses the mechanisms of many human diseases. Using this knowledge, other researchers aim to create new vaccines, antiviral and antibacterial therapies to protect and treat humans across the world.

You can read more about the details of our current work and other aspects of the department, including undergraduate teaching and public outreach activities, on these web pages.

Professor Mark Sansom, Head of Department

News Highlight

How displaceable are water molecules?

Figure: (a) Structure of the bromodomain fold and its conserved water network. (b) Phylogenetic tree of the human bromodomain family, with the 35 bromodomains considered in our study highlighted in green

Figure: (a) Structure of the bromodomain fold and its conserved water network. (b) Phylogenetic tree of the human bromodomain family, with the 35 bromodomains considered in our study highlighted in green
(Click to Enlarge)

The Biggin group, in collaboration with colleagues from the University of Southampton and industry, has just published a large-scale prediction of water-stability in a family of proteins that are key targets for the treatment of many different cancers. Being able to design compounds that displace these key waters is a common strategy in medicinal chemistry, but knowing which waters to target or if they are even likely to be displaceable at all is an extremely challenging problem. The group employ a method, recently developed by the Essex group in Southampton, called Grand Canonical Monte Carlo (GCMC) to make predictions about which water molecules in bromodomains are likely to be displaceable.

Bromodomains are small protein modules that recognise acetylated lysine on histones and thereby regulate gene expression by recruiting various transcription factors. To date, 61 bromodomains have been found in 46 different human proteins. As such, they are being investigated as a promising epigenetic target for diseases like cancer and inflammation. A few bromodomain inhibitors are in fact already in clinical trials for the treatment of leukaemia, midline carcinoma, and progressive lymphoma. Because of this, there is great interest in further exploring the therapeutic potential of this protein family.

Although there is considerable sequence diversity, bromodomains share very similar binding pockets, which makes the discovery of selective probes challenging. Bromodomains are amenable to study by X-ray crystallography and structures are available for many different types of bromodomain (see Figure 1). The structures revealed a conserved water network formed by four water molecules at the base of the binding site (Figure 1) and it is these waters which, if displaceable, may offer opportunities to gain affinity and/or improve selectivity.

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Seminar Professor Fred Hughson, ''chaperoning SNARE assembly to control membrane fusion'' Wednesday 25th Apr, 11:00 Main Seminar Room, New Biochemistry Building
Seminar Dr. Sean Murray, ''Controlling Turing: Self-organisation within bacterial cells'' Wednesday 25th Apr, 13:00 Main Seminar Room, New Biochemistry Building
SBCB Seminar Series William Glass, 'SBCB seminar' Thursday 26th Apr, 14:00 Main Seminar Room, New Biochemistry Building
SBMB Seminar Series Janet Deane, 'Title TBC' Friday 27th Apr, 11:00 Main Seminar Roon, New Biochemistry Building

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