HDAC

Structural studies on protein recognition and regulation

Coordinatore	OULUN YLIOPISTO    more  Organization address address: Pentti Kaiteran Katu 1 city: OULU postcode: 90014 contact info Titolo: Dr. Nome: Leila Cognome: Risteli Email: send email Telefono: +358 8 553 3971 Fax: +358 8 553 3973
Nazionalità Coordinatore	Finland [FI]
Totale costo	45˙000 €
EC contributo	45˙000 €
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-2007-2-2-ERG
Funding Scheme	MC-ERG
Anno di inizio	2008
Periodo (anno-mese-giorno)	2008-03-01   -   2011-02-28

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	OULUN YLIOPISTO  Organization address address: Pentti Kaiteran Katu 1 city: OULU postcode: 90014 contact info Titolo: Dr. Nome: Leila Cognome: Risteli Email: send email Telefono: +358 8 553 3971 Fax: +358 8 553 3973	FI (OULU)	coordinator	0.00

Mappa

 Word cloud

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

 Obiettivo del progetto (Objective)

'With this application, funding is applied for a new project to be started at the Department of Biochemistry, University of Oulu in 2008. The focus of the project will be on structural aspects of protein recognition and regulatory events. To start with, the project will concentrate on selected histone deacetylases and profilins as well as members of the formin family of proteins. X-ray crystallography will be used as the main tool, but the structural work will be complemented by other biochemical and biophysical characterization. Histone deacetylases (HDAC) are, due to their essential role in transcriptional activity as well as many other cellular processes, among the most interesting targets for pharmaceutical research. At present, there is very little information on the structure, specificity, and regulation of various HDACs. This project will focus on structural studies on selected HDACs - to start with HDAC-6, -10, and -11 - and their binding partners. HDAC-6 is a tubulin deacetylase, whereas the biological functions of HDAC-10 and -11 are not very well characterized. In addition to the HDAC catalytic domains, structures of the regulatory domains and binding partners will be pursued. Also inhibitors and substrate-peptides will be used for co-crystallization experiments. Formins are large multi-domain proteins that are involved in the formation of actin filaments by binding to the growing end of actin filaments and e.g. profilins. Diaphanous-related formins are autoregulated, but many other formin family members lack the autoregulatory domains. Many questions remain to be answered concerning the complex regulation of formins and the specificity of different formins with respect to different profilins. Recently, formins have been suggested to affect also microtubule dynamics by co-operating with HDAC-6. The biological significance of this finding remains to be confirmed, but this opens up a new intriguing path to the HDAC and formin field.'