2015 news

We have been busy publishing papers - 9 accepted or already published in the first 6 months of this year.
In a recent Oncotarget paper, we report crystal structures of human IRE1, a drug target in myeloma, that provide a basis for structure-guided design of inhibitors.
Building on our 2014 PNAS paper, we describe the structure of the coiled-coil domain of EML4 in Biochemical Journal.
We have made progress on the regulation of mitotic spindle assembly by Aurora-A and Nek6 kinases through the TACC3 and its binding partners, work published in the Journal of Cell Biology, PLOS Genetics and Biology Open.
These studies are the result of enjoyable and productive collaborations with the groups of Andrew Fry (Leicester), Stephen Royle and Anne Straube (Warwick), Fanni Gergely (CRUK Institute, Cambridge), Jason Chin (MRC-LMB, Cambridge), Mark Pfuhl (Kings College London) and Ian Collins (Institute of Cancer Research, Sutton).

2014 news


Double grant success! Biotechnological and Biological Sciences Research Council (BBSRC) have awarded us a project grant to study the intermicrotubule bridge complex made up of clathrin, ch-TOG and TACC3. Cancer Research UK have awarded us additional funding to develop drugs against multiple myeloma.

Richard Bayliss gave the Frank May Prize Lecture on November 10th 2014. The talk was titled "Molecular medicine: from genes to structures to drugs". link

Structural biology meets stratified medicine in our latest paper, published online in Proc. Natl. Acad. Sci. USA. Mark Richards in my group determined the crystal structure of the human EML1 protein, and teamed up with Ed Law and Sara Busacca in Dean Fennell's group to investigate the structural basis of drug sensitivity in EML4-ALK driven non-small cell lung cancer. We predict how patients might respond to Hsp90 inhibitors that are under clinical evaluation, dependent on the fragment of EML4 present.

Read an article about the collaboration by Cancer Research UK, or press coverage of the paper.

Double grant success! Medical Research Council (MRC) have awarded us a project grant to investigate complexes of proteins that are mutated in polycystic kidney disease. Cancer Research UK have awarded Sameena Khan a Bursary to work on the structural biology of a chemoprevention agent.


2013 news

Working with the team of Stephen Royle in Warwick, we have dissected the interactions within a complex of proteins involved in cell division. This complex provides a new potential target for cancer drugs, a prospect that has been picked up on by Cancer Research UK (here and here), who part-funded our study. Read about this in our paperin the Journal of Cell Biology. Congratulations to Selena and Mark, who are authors on the paper.

How do you switch on a protein kinase using chemistry? What is a good phosphomimic? How do you specify precisely the phosphorylation state of a protein? Finally, which other unnatural amino acids can a ser/thr kinase (auto)-phosphorylate? Find out in our paper in ACS Chemical Biology, joint with Julian Blagg at the Institute of Cancer Research. Congratulations to Fiona, first author on the paper.


Welcome to Patrick McIntyre, the newest member of the team. Patrick studied Chemistry at the University of Reading, and joins us as a graduate student funded by a CASE award from the MRC, sponsored by MRC Technology.


How do kinases switch themselves on? To find out, read our latest paper on kinase autophosphorylation mechanisms in Science Signaling. Congratulations to Charlotte, Sharon and Tammy.

2012 News

Our work on the development of Aurora-A/FLT3 inhibitors as pre-clinical development candidates for the treatment of Acute Myeloid Leukaemia is published on-line at the Journal of Medicinal Chemistry.


Together with Swen Hoelder's group at The Institute of Cancer Research, and Andrew Fry's group here in the Department, we have developed the most potent Nek2-selective inhibitors to date. My group's contribution was on the structure-based design of the inhibitors, which were a hybrid of two previous chemical series. The paper describing our results is now online at the Journal of Medicinal Chemistry, entitled "Design of potent and selective hybrid inhibitors of the mitotic kinase Nek2: SAR, structural biology and cellular activity". Congratulations to the Nek2 team, and especially Corine, Fiona and Sharon from the Bayliss lab.

Our paper that updates our model of Aurora-A activation by phosphorylation and TPX2 is now online in the Journal of Biological Chemistry, entitled "Activation of Aurora-A kinase by protein partner binding (TPX2) and phosphorylation are independent and synergistic".  In this paper, we calculate the energetic contribution of each activator to catalysis and interpret the results in the light of the known crystal structures, a feat that has been achieved for no other protein kinase (as far as we know). Researchers in the mitosis field will be surprised to find that TPX2 can activate unphosphorylated Aurora-A, we certainly were.

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