Structural studies of membrane proteases

Projektinformationen

MEMPROT

ID Finanzhilfevereinbarung: 42486

Startdatum 1 November 2006

Enddatum 31 Oktober 2010

Finanziert unter

• 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

Gesamtkosten € 0,00

EU-Beitrag € 27 582 802,00

Koordiniert durch

INTERNATIONAL INSTITUTE OF MOLECULAR AND CELL BIOLOGY
Poland

Ziel

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.

Wissenschaftliches Gebiet

• engineering and technology › materials engineering › crystals
• natural sciences › biological sciences › biochemistry › biomolecules › proteins
• natural sciences › biological sciences › biochemistry › biomolecules › lipids

Schlüsselbegriffe

• macromolecular structures
• membrane proteins
• small molecule design

Programm/Programme

• 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

Thema/Themen

• MOBILITY-1.3 - Marie Curie Host Fellowships - Transfer of knowledge (TOK)

Aufforderung zur Vorschlagseinreichung

FP6-2005-MOBILITY-3
Andere Projekte für diesen Aufruf anzeigen

Finanzierungsplan

TOK - Marie Curie actions-Transfer of Knowledge

Koordinator

INTERNATIONAL INSTITUTE OF MOLECULAR AND CELL BIOLOGY

• EU-Beitrag: Keine Daten
• Adresse: 4 Ks. Trojdena St. ; WARSAW ; Polen
• Gesamtkosten: Keine Daten

Beteiligte (2)

STOCKHOLM UNIVERSITY

Schweden

• EU-Beitrag: Keine Daten
• Adresse: Universitetsv??A?gen 10A ; STOCKHOLM
• Gesamtkosten: Keine Daten

DIAMOND LIGHT SOURCE

Vereinigtes Königreich

• EU-Beitrag: Keine Daten
• Adresse: Chilton, Didcot ; OXFORDSHIRE
• Gesamtkosten: Keine Daten