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Dr Alun Coker
University College London Division of Medicine
Wolfson Institute for Biomedical Research
London
WC1E 6BT
Tel: 020 7679 6703
Appointment
  • Senior Lecturer
  • Inflammation
  • Div of Medicine
  • Faculty of Medical Sciences
Research Summary

The focus of my work is the use of single crystal X-ray diffraction to determine the three dimensional structure of various proteins and to use these structures to gain an understanding of the protein function at the atomic level and in structure-based drug design.

Current projects:

Norovirus 3C protease. Norovirus is the most common cause of viral gastroenteritis in man and is estimated to cause of around 200,000 deaths/annum predominantly amongst the young, the elderly and the immunocompromised. The noroviral 3C protease (3CLpro) is essential for post-translational maturation of the viral polyprotein and is a validated target. Previously, we have determined the first 3D structure of 3CLpro with a bound inhibitor providing detailed information about the substrate binding site and, more recently, we have used the X-Chem facility at Diamond Light Source to identify drug fragments binding in the active site. We are currently using this information in the rational design of new lead-compounds for drug development.

Dengue/Zika RNA dependant RNA polymerase (RdRp). Dengue and Zika viruses are mosquito-borne Flavivirus of immense global health importance. They have a single-stranded, RNA genome and are dependant on the virally encoded RdRp for replication making it an obvious drug target. The structure of the protein is know for both viruses but the difficulty in preparing and crystallising the protein limit the use of crystallography based rational drug design. We are currently seeking to develop a robust crystallisation platform by engineering highly variable regions of the protein to produce an enzyme optimised for ease of purification and crystallisation.

Cyclophilin D and the Mitochondrial Permeability Transition Pore (PTP). Formation of the mitochondrial permeability transition pore is a key step in apoptosis. Although the formation and structure of the pore is poorly understood CypD has been identified as a key component. Both ablation of the CypD gene and inhibition of CypD have been shown to inhibit MTP formation and apoptosis; CypD therefore presents an attractive target for drugs to treat a wide range of diseases (such as multipleswhere apoptosis We have been working with David Selwood's medicinal chemistry, providing crystallography support to their drug-design program which has identified an number of promising inhibiotors of CypD.



Teaching Summary

Undergraduate Teaching

I am co-director of the iBSc in Clinical Sciences where I lecture and run practicals.

I deliver crystallography lectures on the pharmacology Drug Design and Development module.

I typically host two to three undergraduate project students a year from the iBSc Clinical Sciences programme and from various other BSc programmes.


Postgraduate Teaching

I lecture and run practicals on the MSc Drug Design.

I am programme lead for the MSc Advanced Biomedical Imaging.

I typically host two to three masters project students from the MSc Drug Design each year.

Academic Background
1998 PhD Doctor of Philosophy – Protein Crystallography Birkbeck College
1990 MSc Master of Science – Biomolecular Organisation Birkbeck College
1986 BSc Bachelor of Science – Biomolecular Science University of Portsmouth
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