Objectif Proteases are key players in many cellular processes and come in great variety. There are essentially five different catalytic types: serine/threonine, cysteine, aspartic and metallopeptidases. Each type of active site can be found in several different folds, which suggests that active sites have been reinvented multiple times during evolution. The soluble peptidase folds have been studied in great detail, and in nearly all cases, at least one prototype crystal structure is available. In contrast, there are almost no crystal structures of integral membrane proteases, therefore their mechanistic understanding lies far behind. It is not even clear whether a specific water channel is required to transport a catalytic water molecule to the active site or whether a low concentration of water in the lipid bilayer is sufficient for amide cleavage. Despite these uncertainties, the combined results of sequence comparisons and biochemical studies suggest that membrane and soluble proteases will probably turn out to have (a) dissimilar folds and (b) similar active sites. However, there is no good evidence yet for a membrane-embedded cysteine peptidase, and for several membrane protease families the assignment of the catalytic type is controversial, which may be an indication for a novel type of active site. In order to broaden the spectrum of our research we are planning to acquire new skills in membrane protein overexpression, purification and crystallization which we would then apply for structural studies of membrane proteases. Champ scientifique engineering and technologymaterials engineeringcrystalsnatural sciencesbiological sciencesbiochemistrybiomoleculesproteinsnatural sciencesbiological sciencesbiochemistrybiomoleculeslipids Mots‑clés macromolecular structures membrane proteins small molecule design Programme(s) FP6-MOBILITY - Human resources and Mobility in the specific programme for research, technological development and demonstration "Structuring the European Research Area" under the Sixth Framework Programme 2002-2006 Thème(s) MOBILITY-1.3 - Marie Curie Host Fellowships - Transfer of knowledge (TOK) Appel à propositions FP6-2005-MOBILITY-3 Voir d’autres projets de cet appel Régime de financement TOK - Marie Curie actions-Transfer of Knowledge Coordinateur INTERNATIONAL INSTITUTE OF MOLECULAR AND CELL BIOLOGY Contribution de l’UE Aucune donnée Adresse 4 Ks. Trojdena St. WARSAW Pologne Voir sur la carte Liens Site web Opens in new window Coût total Aucune donnée Participants (2) Trier par ordre alphabétique Trier par contribution de l’UE Tout développer Tout réduire STOCKHOLM UNIVERSITY Suède Contribution de l’UE Aucune donnée Adresse Universitetsv??A?gen 10A STOCKHOLM Voir sur la carte Liens Site web Opens in new window Coût total Aucune donnée DIAMOND LIGHT SOURCE Royaume-Uni Contribution de l’UE Aucune donnée Adresse Chilton, Didcot OXFORDSHIRE Voir sur la carte Liens Site web Opens in new window Coût total Aucune donnée