P-TYPE ATPASES

Structural studies of P-type ATPases and their characterization in native membranes

 Coordinatore AARHUS UNIVERSITET 

 Organization address address: Nordre Ringgade 1
city: AARHUS C
postcode: 8000

contact info
Titolo: Prof.
Nome: Poul
Cognome: Nissen
Email: send email
Telefono: -13922
Fax: -11745

 Nazionalità Coordinatore Denmark [DK]
 Totale costo 203˙817 €
 EC contributo 203˙817 €
 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-IEF-2008
 Funding Scheme MC-IEF
 Anno di inizio 2009
 Periodo (anno-mese-giorno) 2009-04-01   -   2009-12-31

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    AARHUS UNIVERSITET

 Organization address address: Nordre Ringgade 1
city: AARHUS C
postcode: 8000

contact info
Titolo: Prof.
Nome: Poul
Cognome: Nissen
Email: send email
Telefono: -13922
Fax: -11745

DK (AARHUS C) coordinator 203˙817.53

Mappa


 Word cloud

Esplora la "nuvola delle parole (Word Cloud) per avere un'idea di massima del progetto.

protein    membranes    crystallography    pumps    ca    structure       na    atpase    pmca    native    determine    environment    cation    complexes    plan    atpases    membrane   

 Obiettivo del progetto (Objective)

'P-type ATPases are cell-membrane pumps that are of fundamental importance in eukaryotes. The ion gradients created by Ca2-ATPases or Na,K-ATPases are involved in signalling, maintaining the membrane potential as well as secondary active transport. Despite the recent progress in membrane protein crystallography, the lack of detailed structural information currently prevents a better understanding of function and specificity of cation pumps. One specific aim of this proposed research is to determine the structure of the plasma-membrane Ca2-ATPase (PMCA) and to understand its regulatory mechanism. The autoinhibited PMCA will be recombinantly expressed in yeast, purified and crystallized. In addition, it is also planned to determine the structure of the activated complex consisting of PMCA and calcium-bound calmodulin (Ca2-CaM). In order to deepen our understanding of cation pumps in their native environment, I further propose to investigate Na,K-ATPases in native membranes using a multi-technique approach. First, I will analyze complexes of Na,K-ATPase isolated from native membranes by mass spectrometry to identify peripheral proteins. In the next step, I plan to assemble those identified multi-protein complexes in vitro and structurally characterize them by cryo-EM. Finally, I plan to use AFM to investigate the oligomeric arrangement of Na,K-ATPases in native membranes. This multi-disciplinary project will hopefully expand our knowledge of cation pumps by putting atomic details in the context of the native environment and will concurrently allow me to gain experience in membrane protein crystallography that will complement my expertise in biophysical methods.'

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