Discovery of peptide ligands targeting a specific ubiquitin-like domain-binding site in the deubiquitinase USP11 (2018)
Journal Article
Spiliotopoulos, A., Blokpoel Ferreras, L., Densham, R. M., Caulton, S. G., Maddison, B. C., Morris, J. R., …Dreveny, I. (in press). Discovery of peptide ligands targeting a specific ubiquitin-like domain-binding site in the deubiquitinase USP11. Journal of Biological Chemistry, doi:10.1074/jbc.ra118.004469

Ubiquitin specific proteases (USPs) reverse ubiquitination and regulate virtually all cellular processes. Defined non-catalytic domains in USP4 and USP15 are known to interact with E3 ligases and substrate recruitment factors. No such interactions ha... Read More

The structure of the deubiquitinase USP15 reveals a misaligned catalytic triad and an open ubiquitin-binding channel (2018)
Journal Article
Ward, S. J., Gratton, H. E., Indrayudha, P., Michavila, C., Mukhopadhyay, R., Maurer, S. K., …Dreveny, I. (2018). The structure of the deubiquitinase USP15 reveals a misaligned catalytic triad and an open ubiquitin-binding channel. Journal of Biological Chemistry, 293(45), 17362-17374. doi:10.1074/jbc.ra118.003857

Ubiquitin specific protease 15 (USP15) regulates important cellular processes, including transforming growth factor β (TGF-β) signaling, mitophagy, mRNA processing, and innate immune responses; however, structural information on USP15’s catalytic dom... Read More

Identification of lipases with activity towards monoacylglycerol by criterion of conserved cap architectures (2018)
Journal Article
Riegler-Berket, L., Leitmeier, A., Aschauer, P., Dreveny, I., & Oberer, M. (in press). Identification of lipases with activity towards monoacylglycerol by criterion of conserved cap architectures. BBA - Biochimica et Biophysica Acta, 1863(7), ISSN 0006-3002

Monoacylglycerol lipases (MGL) are a subclass of lipases that predominantly hydrolyze monoacylglycerol (MG) into glycerol and fatty acid. MGLs are ubiquitous enzymes across species and play a role in lipid metabolism, affecting energy homeostasis and... Read More

PqsBC, a condensing enzyme in the biosynthesis of the Pseudomonas aeruginosa quinolone signal: crystal structure, inhibition, and reaction mechanism (2016)
Journal Article
Drees, S. L., Li, C., Prasetya, F., Saleem, M., Dreveny, I., Williams, P., …Fetzner, S. (2016). PqsBC, a condensing enzyme in the biosynthesis of the Pseudomonas aeruginosa quinolone signal: crystal structure, inhibition, and reaction mechanism. Journal of Biological Chemistry, 291(13), doi:10.1074/jbc.M115.708453. ISSN 0021-9258

Pseudomonas aeruginosa produces a number of alkylquinolone-type secondary metabolites best known for their antimicrobial effects and involvement in cell-cell communication. In the alkylquinolone biosynthetic pathway, the β-ketoacyl-(acyl carrier prot... Read More

Sensitive recovery of recombinant antibody clones after their in silico identification within NGS datasets (2015)
Journal Article
Spiliotopoulos, A., Owen, J. P., Maddison, B. C., Dreveny, I., Rees, H. C., & Gough, K. C. (2015). Sensitive recovery of recombinant antibody clones after their in silico identification within NGS datasets. Journal of Immunological Methods, 420, doi:10.1016/j.jim.2015.03.005. ISSN 0022-1759

Recently the analytical power of the latest high throughput next generation DNA sequencing platforms has been used to analyse phage that have been selected from the panning of large combinatorial libraries displaying either peptide or antibody ligand... Read More

Coagulation factor XII protease domain crystal structure (2015)
Journal Article
Pathak, M., Wilmann, P., Awford, J., Li, C., Hamad, B., Fischer, P., …Emsley, J. (2015). Coagulation factor XII protease domain crystal structure. Journal of Thrombosis and Haemostasis, 13(4), 580-591. doi:10.1111/jth.12849

Background: Coagulation factor XII is a serine protease that is important for kinin generation and blood coagulation, cleaving the substrates plasma kallikrein and FXI. Objective: To investigate FXII zymogen activation and substrate recognition by d... Read More

Structure and catalytic regulatory function of ubiquitin specific protease 11 N-terminal and ubiquitin-like domains (2014)
Journal Article
Harper, S., Gratton, H. E., Cornaciu, I., Oberer, M., Scott, D. J., Emsley, J., & Dreveny, I. (in press). Structure and catalytic regulatory function of ubiquitin specific protease 11 N-terminal and ubiquitin-like domains. Biochemistry, 53(18), doi:10.1021/bi500116x. ISSN 1520-4995

The ubiquitin specific protease 11 (USP11) is implicated in DNA repair, viral RNA replication, and TGFβ signaling. We report the first characterization of the USP11 domain architecture and its role in regulating the enzymatic activity. USP11 consists... Read More

The double PHD finger domain of MOZ/MYST3 induces α-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification (2014)
Journal Article
Dreveny, I., Deeves, S. E., Fulton, J., Yue, B., Messmer, M., Bhattacharya, A., …Heery, D. M. (2014). The double PHD finger domain of MOZ/MYST3 induces α-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification. Nucleic Acids Research, 42(2), doi:10.1093/nar/gkt931. ISSN 0305-1048

Histone tail modifications control many nuclear processes by dictating the dynamic exchange of regulatory proteins on chromatin. Here we report novel insights into histone H3 tail structure in complex with the double PHD finger (DPF) of the lysine ac... Read More