Skip to main content
ISTH 2023 Main banner
Back

    Jonas Emsley, Phd

    Professor
    Nottingham Biodiscovery Institute, School of Pharmacy
    Nottingham, England, United Kingdom

    Dr Jonas Emsley
    Professor of Macromolecular Crystallography,
    email:jonas.emsley@nottingham.ac.uk
    http://www.nottingham.ac.uk/research/groups/structural-biology/index.aspx
    https://orcid.org/0000-0002-8949-8030

    My research focuses on investigating the complex biological processes of blood hemostasis and thrombosis with a special interest in the co-operation of different blood cell types and plasma proteins with a focus on molecular structure. . A major focus in recent years is the structure of plasma proteases to elucidate the mechanism of latency, substrate recognition, selectivity, co-factor/membrane lipid interactions and inhibitor design. JE group has published the first crystal structure of coagulation factor XI protease in complex with a peptide from the co-factor HK (Blood 2016) which shows the enzyme in a latent conformation. JE group has recently solved the first example of structure in an active conformation of the related apple domain containing protease prekallikrein (JTH 2019-front cover, Blood 2020) which revealed a major 180 degree rotational conformational change termed apple domain disc rotation. We have also determined prekallikrein-substrate complex crystal structures (manuscript drafted). Also my group reported the first crystal structure of the Factor XII (FXII) protease (JTH 2015) which revealed a latent conformation and more recently the active form in complex with peptidomimetic inhibitor (Acta Cryst in press 2019). I was involved in modelling the partially latent structure of the single chain FXII active site (Blood 2017). Recent structures include the complement receptor-FXII complex (manuscript in revision Blood 2020. I have advanced understanding of the field of cell receptor structural biology for ~25 years and contributed to greater understanding of the molecular basis of cell receptor ligand interactions for both extracellular domains forming connections to the extracellular matrix [1,10] and intracellular domains which form connections to the cytoskeleton (PMID: 15642262, PMID: 15272303, PMID: 16135522, PMID: 16407302).

    Presentation(s):