INTRAMEMPROT
Mechanistic and structural insight into di-aspartyl intramembrane proteases
| Coordinatore | CENTRE NATIONAL DE LA RECHERCHE SCIENTIFIQUE
Organization address
address: Rue Michel -Ange 3 contact info |
| Nazionalità Coordinatore | France [FR] |
| Totale costo | 239˙918 € |
| EC contributo | 239˙918 € |
| Programma | FP7-PEOPLE
Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013) |
| Code Call | FP7-PEOPLE-2009-IOF |
| Funding Scheme | MC-IOF |
| Anno di inizio | 2011 |
| Periodo (anno-mese-giorno) | 2011-04-01 - 2014-03-31 |
Partecipanti
| # | ||||
|---|---|---|---|---|
| 1 |
CENTRE NATIONAL DE LA RECHERCHE SCIENTIFIQUE
Organization address
address: Rue Michel -Ange 3 contact info |
FR (PARIS) | coordinator | 239˙918.20 |
Mappa
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Obiettivo del progetto (Objective)
'The proposed project aims at providing structural and functional characterization of a family of membrane proteins from archaea, which are either homologous or related in structure to the human protein Presenilin. Membrane proteins represent one third of the proteins of living organisms, one half of drug targets, and still less than 1% of known protein structures refers to this class of macromolecules. The successful accomplishment of such a project will possibly result in a fundamental progress, contributing to the understanding of a widespread, still puzzling biological process (intra-membrane proteolysis), and of the molecular mechanisms of related pathologies (such as Alzheimer’s disease). This fellowship will give the candidate the opportunity to acquire the complementary skills necessary to consolidate his expertise in membrane protein research, by attending one of the most outstanding research institutions worldwide (Columbia University). He will then be able to enter a phase of concrete professional independence and maturity. The know-how acquired by the fellow will contribute, as well, to enrich the range of methodological approaches available at the Return Host Institution, which studies membrane proteins by means of different complementary techniques. Paving the way to future collaborations, it will also contribute to European excellence. Membrane protein studies, in fact, are amongst the most challenging in the field of structural biology and biochemistry. Preliminary results are so encouraging, that structural characterization represents a possible goal, whereas functional data will provide an added value or an assured backup. Some novel approaches, developed at the Outgoing Institution, might represent unprecedented tools, useful to tackle this field of the biological research, and answer to an urgent, imperative need: understanding membrane protein functioning.'
Introduzione (Teaser)
Unveiling the enzymatic activity of proteins requires the identification of substrate binding domains and conformational changes incurred during the reaction. This necessitates delineation of the 3D protein structure, which is experimentally achieved through crystallography.