• Publications
  • Influence
Human β-tryptase is a ring-like tetramer with active sites facing a central pore
Human tryptase, a mast-cell-specific serine proteinase that may be involved in causing asthma and other allergic and inflammatory disorders, is unique in two respects: it is enzymatically active onlyExpand
Isolation, Cloning and Structural Characterisation of Boophilin, a Multifunctional Kunitz-Type Proteinase Inhibitor from the Cattle Tick
The crystal structure of the bovine α-thrombin·boophilin·trypsin complex, refined at 2.35 Å resolution reveals a non-canonical binding mode to the proteinase, and suggests a mechanism for prothrominase inhibition in vivo. Expand
The structure of the human betaII-tryptase tetramer: fo(u)r better or worse.
The structure of the 3-A crystal structure of human betaII-tryptase in complex with 4-amidinophenylpyruvic acid provides an improved understanding of the unique properties of the biologically active tryptase tetramer in solution and will be an incentive for the rational design of mono- and multifunctionaltryptase inhibitors. Expand
The Apoptogenic Toxin AIP56 Is a Metalloprotease A-B Toxin that Cleaves NF-κb P65
This work demonstrates that AIP56 is an A-B toxin capable of acting at distance, without requiring contact of the bacteria with the target cell, and shows that the N-terminal domain cleaves NF-κB at the Cys39-Glu40 peptide bond and that the C-terminals are involved in binding and internalization into the cytosol. Expand
Sea bass (Dicentrarchus labrax) invariant chain and class II major histocompatibility complex: sequencing and structural analysis using 3D homology modelling.
The present manuscript reports for the first time the sequencing and characterisation of sea bass (sb) MHCII alpha and beta chains and Ii chain cDNAs as well as their expression analysis underExpand
Crystal structure of the human α‐thrombin–haemadin complex: an exosite II‐binding inhibitor
Haemadin binds to thrombin according to a novel mechanism, despite an overall structural similarity with hirudin, which makes it an ideal candidate for an antithrombotic agent, as well as a starting point for the design of novel antithromabotics. Expand
Specific inhibition of insect α-amylases: yellow meal worm α-amylase in complex with the Amaranth α-amylase inhibitor at 2.0 Å resolution
The binding of AAI to TMA presents a new inhibition mode for α -amylases and opens new perspectives for the engineering of various novel activities onto the small scaffold of this group of proteins. Expand
Caspase-1 and IL-1β Processing in a Teleost Fish
It is shown that sea bass caspase-1 auto-processing is similar to that of the human enzyme, resulting in active p24/p10 and p20/ p10 heterodimers, and it is shown That sea bass and avian IL-1β are specifically cleaved by caspases at different but phylogenetically conserved aspartates, distinct from the cleavage site of mammalian IL- 1β. Expand
Unveiling the structural basis for translational ambiguity tolerance in a human fungal pathogen
This study provides a first detailed analysis on natural reassignment of codon identity, unveiling a highly dynamic evolutionary pattern of thousands of fungal CUG codons to confer an optimized balance between protein structural robustness and functional plasticity. Expand
Human beta-tryptase is a ring-like tetramer with active sites facing a central pore.
The nature of this unique tetrameric architecture explains many of tryptase's biochemical properties and provides a basis for the rational design of monofunctional and bifunctionaltryptase inhibitors. Expand