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We use X-ray crystallography and other biochemical methods to understand reaction mechanisms and structural features of metabolic enzyme protein families.

Our interests center around oxidoreductive enzyme families such as short-chain dehydrogenases/reductases (SDR), or α-ketoglutarate dependent oxygenases, the latter of importance in chromatin modification such as histone demethylation. Other areas include elucidation of structure-activity relationships of mevalonate pathway enzymes or proteases involved in antigen presentation and immunity. Together with chemistry collaborators we develop chemical tools and use these to understand the catalytic mechanism and ligand features of these enzyme classes.

Ribbon diagram

Ribbon diagram of the catalytic domain of human JmjD2A (KDM4), a member of the α-ketoglutarate dependent histone demethylase family.

Phylogenetic tree

Phylogenetic tree of human short-chain dehydrogenases – a metabolic protein superfamily. Red dots indicate structure determination by X-ray crystallography solved by our group at the Structural Genomics Consortium.

Structure of human ERAP1

Structure of human ERAP1

Endoplasmatic reticulum aminopeptidase 1 (ERAP1) is a multifunctional enzyme involved in trimming of peptides to an optimal length for presentation by major histocompatibility complex (MHC) class I molecules. Surface model and mapping of residues of single nucleotide polymorphisms associated with Ankylosing spondylitis.

Structure of human FPPS

Structure of human FPPS

Farnesylpyrophosphate synthase (FPPS) is a key step in isoprenoid synthesis and the molecular target of nitrogen containing bisphosphonates, of clinical use in conditions of excessive bone resorption such as osteoporosis, Paget's disease or cancer of the bone. We have solved the X-ray structures of human FPPS and provided detailed snapshots and insights into structure-activity relationships of this drug target.


Kathryn Kavanagh

Wyatt Yue

Petra Lukacik

Naeem Shafqat

Stan Ng

Ewa Pilka

Grazyna Kochan

Maria Tsoumpra