Objetivo 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. Ámbito científico engineering and technologymaterials engineeringcrystalsnatural sciencesbiological sciencesbiochemistrybiomoleculesproteinsnatural sciencesbiological sciencesbiochemistrybiomoleculeslipids Palabras clave macromolecular structures membrane proteins small molecule design Programa(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 Tema(s) MOBILITY-1.3 - Marie Curie Host Fellowships - Transfer of knowledge (TOK) Convocatoria de propuestas FP6-2005-MOBILITY-3 Consulte otros proyectos de esta convocatoria Régimen de financiación TOK - Marie Curie actions-Transfer of Knowledge Coordinador INTERNATIONAL INSTITUTE OF MOLECULAR AND CELL BIOLOGY Aportación de la UE Sin datos Dirección 4 Ks. Trojdena St. WARSAW Polonia Ver en el mapa Enlaces Sitio web Opens in new window Coste total Sin datos Participantes (2) Ordenar alfabéticamente Ordenar por aportación de la UE Ampliar todo Contraer todo STOCKHOLM UNIVERSITY Suecia Aportación de la UE Sin datos Dirección Universitetsv??A?gen 10A STOCKHOLM Ver en el mapa Enlaces Sitio web Opens in new window Coste total Sin datos DIAMOND LIGHT SOURCE Reino Unido Aportación de la UE Sin datos Dirección Chilton, Didcot OXFORDSHIRE Ver en el mapa Enlaces Sitio web Opens in new window Coste total Sin datos
