Heterotypic Sam-Sam association between Odin-Sam1 and Arap3-Sam: binding affinity and structural insights. (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• Heterotypic Sam-Sam association between Odin-Sam1 and Arap3-Sam: binding affinity and structural insights. (Articolo in rivista) (literal)

Anno

• 2013-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1002/cbic.201200592 (literal)

Alternative label

• Flavia Anna Mercurio, Daniela Marasco, Luciano Pirone, Pasqualina Liana Scognamiglio, Emilia Maria Pedone, Maurizio Pellecchia, Marilisa Leone (2013)
  Heterotypic Sam-Sam association between Odin-Sam1 and Arap3-Sam: binding affinity and structural insights.
  in ChemBioChem (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Flavia Anna Mercurio, Daniela Marasco, Luciano Pirone, Pasqualina Liana Scognamiglio, Emilia Maria Pedone, Maurizio Pellecchia, Marilisa Leone (literal)

Pagina inizio

• 100 (literal)

Pagina fine

• 106 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 14 (literal)

Rivista

• ChemBioChem (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

• 1 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Department of Biological Sciences, University of Naples Federico II, Via Mezzocannone 16, 80134 Naples, Italy Sanford|Burnham Medical Research Institute, La Jolla, CA (literal)

Titolo

• Heterotypic Sam-Sam association between Odin-Sam1 and Arap3-Sam: binding affinity and structural insights. (literal)

Abstract

• Arap3 is a phosphatidylinositol 3 kinase effector protein that plays a role as GTPase activator (GAP) for Arf6 and RhoA. Arap3 contains a sterile alpha motif (Sam) domain that has high sequence homology with the Sam domain of the EphA2-receptor (EphA2-Sam). Both Arap3-Sam and EphA2-Sam are able to associate with the Sam domain of the lipid phosphatase Ship2 (Ship2-Sam). Recently, we reported a novel interaction between the first Sam domain of Odin (Odin-Sam1), a protein belonging to the ANKS (ANKyrin repeat and Sam domain containing) family, and EphA2-Sam. In our latest work, we applied NMR spectroscopy, surface plasmon resonance (SPR) and isothermal titration calorimetry (ITC) to characterize the association between Arap3-Sam and Odin-Sam1. We show that these two Sam domains interact with low micromolar affinity. Moreover, by means of molecular docking techniques, supported by NMR data, we demonstrate that Odin-Sam1 and Arap3-Sam might bind with a topology that is common to several Sam-Sam complexes. The revealed structural details form the basis for the design of potential peptide antagonists that could be used as chemical tools to investigate functional aspects related to heterotypic Arap3-Sam associations. (literal)

Prodotto di

• Institute of biostructure and bioimaging (IBB) (Istituto)
• Institute of Crystallography (IC) (Istituto)
• Determinazione della struttura tridimensionale di biomolecole complesse con tecniche spettroscopiche e cristallografiche (PM.P01.022.001) (Modulo)

Autore CNR

• MARILISA LEONE (Persona)
• EMILIA MARIA PEDONE (Unità di personale interno)
• LUCIANO PIRONE (Unità di personale esterno)

Incoming links:

Prodotto

• Institute of Crystallography (IC) (Istituto)
• Institute of biostructure and bioimaging (IBB) (Istituto)
• Determinazione della struttura tridimensionale di biomolecole complesse con tecniche spettroscopiche e cristallografiche (PM.P01.022.001) (Modulo)

Autore CNR di

• EMILIA MARIA PEDONE (Unità di personale interno)
• MARILISA LEONE (Persona)
• LUCIANO PIRONE (Unità di personale esterno)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• ChemBioChem (Rivista)