http://www.cnr.it/ontology/cnr/individuo/prodotto/ID206083
Structure prediction and validation of the ERK8 kinase domain (Articolo in rivista)
- Type
- Label
- Structure prediction and validation of the ERK8 kinase domain (Articolo in rivista) (literal)
- Anno
- 2013-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1371/journal.pone.0052011 (literal)
- Alternative label
Strambi A, Mori M, Rossi M, Colecchia D, Manetti F, Carlomagno F, Botta M and Chiariello M (2013)
Structure prediction and validation of the ERK8 kinase domain
in PloS one
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Strambi A, Mori M, Rossi M, Colecchia D, Manetti F, Carlomagno F, Botta M and Chiariello M (literal)
- Pagina inizio
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Istituto Toscano Tumori-Core Research Laboratory, Signal Transduction Unit, AOU Senese, Siena, Italy
Istituto di Fisiologia Clinica, Consiglio Nazionale delle Ricerche (CNR), Siena, Italy
Dipartimento Farmaco Chimico Tecnologico, Università degli Studi di Siena, Siena, Italy
Università degli Studi di Siena, Siena, Italy
Dipartimento di Biologia e Patologia Cellulare e Molecolare, Università degli Studi di Napoli, Napoli, Italy (literal)
- Titolo
- Structure prediction and validation of the ERK8 kinase domain (literal)
- Abstract
- Extracellular signal-regulated kinase 8 (ERK8) has been already implicated in cell transformation and in the protection of genomic integrity and, therefore, proposed as a novel potential therapeutic target for cancer. In the absence of a crystal structure, we developed a three-dimensional model for its kinase domain. To validate our model we applied a structure- based virtual screening protocol consisting of pharmacophore screening and molecular docking. Experimental characterization of the hit compounds confirmed that a high percentage of the identified scaffolds was able to inhibit ERK8. We also confirmed an ATP competitive mechanism of action for the two best-performing molecules. Ultimately, we identified an ERK8 drug-resistant ''gatekeeper'' mutant that corroborated the predicted molecular binding mode, confirming the reliability of the generated structure. We expect that our model will be a valuable tool for the development of specific ERK8 kinase inhibitors. (literal)
- Prodotto di
- Autore CNR
Incoming links:
- Autore CNR di
- Prodotto
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi