HKMTIS

Computer-aided Design and synthesis of inhibitors of EED-EZH2 interaction as a novel approach for anticancer therapy

Coordinatore	IMPERIAL COLLEGE OF SCIENCE, TECHNOLOGY AND MEDICINE    more  Organization address address: SOUTH KENSINGTON CAMPUS EXHIBITION ROAD city: LONDON postcode: SW7 2AZ contact info Titolo: Ms. Nome: Brooke Cognome: Alasya Email: send email Telefono: +44 207 594 1181 Fax: +44 207 594 1418
Nazionalità Coordinatore	United Kingdom [UK]
Totale costo	209˙033 €
EC contributo	209˙033 €
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-2011-IIF
Funding Scheme	MC-IIF
Anno di inizio	2013
Periodo (anno-mese-giorno)	2013-04-03   -   2015-04-02

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	IMPERIAL COLLEGE OF SCIENCE, TECHNOLOGY AND MEDICINE  Organization address address: SOUTH KENSINGTON CAMPUS EXHIBITION ROAD city: LONDON postcode: SW7 2AZ contact info Titolo: Ms. Nome: Brooke Cognome: Alasya Email: send email Telefono: +44 207 594 1181 Fax: +44 207 594 1418	UK (LONDON)	coordinator	209˙033.40

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 Obiettivo del progetto (Objective)

'The Polycomb repressive complex (PRC2) complex catalyzes the trimethylation of lysine 27 on histone H3 (H3K27me3), which is an important epigenetic mark for maintaining transcriptional repression. The interaction between the two of the components, EED and EZH2, of PRC2 is essential for the required histone lysine methyltransferase (HKMTase) activity that resides in the SET-domain of EZH2. We propose to design the inhibitors of EED-EZH2 interaction using the recently reported X-ray crystal structure of the complex and employing computational drug design methods. A stepwise rational approach will be employed that would involve, identifying a binding sites around the important amino acid residues of EED, structure-based pharmacophore generation, virtual screening, structure optimization and biological screening, in order to discovery the novel HKMTase inhibitors'