Cel 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. Dziedzina nauki engineering and technologymaterials engineeringcrystalsnatural sciencesbiological sciencesbiochemistrybiomoleculesproteinsnatural sciencesbiological sciencesbiochemistrybiomoleculeslipids Słowa kluczowe macromolecular structures membrane proteins small molecule design Program(-y) 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 Temat(-y) MOBILITY-1.3 - Marie Curie Host Fellowships - Transfer of knowledge (TOK) Zaproszenie do składania wniosków FP6-2005-MOBILITY-3 Zobacz inne projekty w ramach tego zaproszenia System finansowania TOK - Marie Curie actions-Transfer of Knowledge Koordynator INTERNATIONAL INSTITUTE OF MOLECULAR AND CELL BIOLOGY Wkład UE Brak danych Adres 4 Ks. Trojdena St. WARSAW Polska Zobacz na mapie Linki Strona internetowa Opens in new window Koszt całkowity Brak danych Uczestnicy (2) Sortuj alfabetycznie Sortuj według wkładu UE Rozwiń wszystko Zwiń wszystko STOCKHOLM UNIVERSITY Szwecja Wkład UE Brak danych Adres Universitetsv??A?gen 10A STOCKHOLM Zobacz na mapie Linki Strona internetowa Opens in new window Koszt całkowity Brak danych DIAMOND LIGHT SOURCE Zjednoczone Królestwo Wkład UE Brak danych Adres Chilton, Didcot OXFORDSHIRE Zobacz na mapie Linki Strona internetowa Opens in new window Koszt całkowity Brak danych