Henry Wellcome Building of Genomic Medicine
|The structure of the RPTPmu trans dimer (Aricescu et al Science 2007)|
|Semaphorin-plexin recognition complex (Janssen et al Nature 2010)|
E. Yvonne Jones
The Sir Andrew McMichael Professor of Structural Immunology
Yvonne Jones is co-Head of STRUBI and Deputy Head of the NDM. Her own research group is focused on the structural biology of extracellular recognition and signalling complexes. The group's core techniques include protein crystallography and cryo electron microscopy, which are used to generate high resolution structural information. Importantly, studies using these techniques are integrated with advanced light microscopy and cryo electron tomography, as well as cell-based functional studies, to probe molecular mechanisms at the cell surface.
The group's research addresses fundamental questions about cell-cell signalling systems of importance to human health. How are signalling assemblies arranged? Which features are necessary for normal signal transduction into the cell? What mechanisms trigger dysfunctional signalling? The work ties into an extensive network of interdisciplinary local and international collaborations with the ultimate aim of learning how to manipulate these signalling systems for the design of new clinical therapies. Current projects within the group focus on signalling systems of importance in developmental biology. These include semaphorin/plexin/neuropilin ligand-receptor complexes involved in cell guidance as well as mechanisms controlling signalling by the Wnt family of morphogens.
Mouse and human antibodies bind HLA-E-leader peptide complexes and enhance NK cell cytotoxicity.
Li D. et al, (2022), Commun Biol, 5
Virtual Screening Directly Identifies New Fragment-Sized Inhibitors of Carboxylesterase Notum with Nanomolar Activity
Steadman D. et al, (2021), Journal of Medicinal Chemistry
Small-molecule inhibitors of carboxylesterase Notum
Zhao Y. et al, (2021), Future Medicinal Chemistry
Notum Deacylates Octanoylated Ghrelin
Zhao Y. et al, (2021), Molecular Metabolism, 101201 - 101201
Caffeine inhibits Notum activity by binding at the catalytic pocket
Zhao Y. et al, (2020), Communications Biology, 3